|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
1.40e-105 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 336.48 E-value: 1.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 31982223 283 RG 284
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-284 |
2.69e-84 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 276.16 E-value: 2.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWHVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136 151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 31982223 277 LYELVIRG 284
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1728-1799 |
2.48e-38 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 137.96 E-value: 2.48e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1728 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1799
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1446-1787 |
7.95e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1525
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKA 1605
Cdd:COG1196 320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1606 ETVQAALEEAQRAQGAAQgaiwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRagnsLAASTA 1685
Cdd:COG1196 378 EEELEELAEELLEALRAA----------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1686 EETAGSAQSRAREAEKQLREQVGDQyQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGtyEENER 1765
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLR 520
|
330 340
....*....|....*....|..
gi 31982223 1766 ALEGKAAQLDGLEARMRSVLQA 1787
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEA 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1463-1788 |
2.88e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.09 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1463 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1534
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1535 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAHRARSRAEGERQKAE 1606
Cdd:PRK02224 290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1607 TVQAALEEAQRAQGAAQGAI--------------WGAVVDTQNTE-------QTLQRVQERMAGAEKSLNSAGERARQLD 1665
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIeeleeeieelrerfGDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1666 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1712
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1713 TVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEaRMRSVLQAI 1788
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1472-1794 |
9.75e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.49 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1472 GGILSR---VSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsQEGADPDSIEMVATRvldISIPA 1548
Cdd:TIGR02168 670 SSILERrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQISALR---KDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1549 SPEQIQRLASEIAERVRSLADVDtilAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIwg 1628
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-- 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1629 avvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAgnSLAASTAEEtagsaQSRAREAEKQLrEQVG 1708
Cdd:TIGR02168 813 -----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--SLAAEIEEL-----EELIEELESEL-EALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1709 DQYQTVRALAERkaegvlaAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQaI 1788
Cdd:TIGR02168 880 NERASLEEALAL-------LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-L 951
|
....*.
gi 31982223 1789 NLQVQI 1794
Cdd:TIGR02168 952 TLEEAE 957
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
784-829 |
1.13e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.13e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 784 CQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGFGPAGC 829
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
784-832 |
1.32e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 1.32e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 784 CQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGFGPAGCQAC 832
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
783-830 |
1.83e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 1.83e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 783 PCQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGF--GPAGCQ 830
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1480-1767 |
1.43e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 69.85 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1480 ETRRQAEEAQQRAQAALDKANASRGQV-EQANQELRELIQNVKDFLSQEGADPDSIEMVATrvldisipaspEQIQRLAS 1558
Cdd:NF041483 441 EARRLRGEAEQLRAEAVAEGERIRGEArREAVQQIEEAARTAEELLTKAKADADELRSTAT-----------AESERVRT 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1559 EIAERVRSLAdvdtilahtmgdvRRAEQLLQdahraRSRAEGERQKAEtvqaALEEAQRAQGAAQGAiwgAVVDTQNTEQ 1638
Cdd:NF041483 510 EAIERATTLR-------------RQAEETLE-----RTRAEAERLRAE----AEEQAEEVRAAAERA---ARELREETER 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1639 T-----------LQRVQ----ERMAGAEKSLNSA---GERARQlDALLEALKLK-------RAGNSLAASTAE----ETA 1689
Cdd:NF041483 565 AiaarqaeaaeeLTRLHteaeERLTAAEEALADAraeAERIRR-EAAEETERLRteaaeriRTLQAQAEQEAErlrtEAA 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1690 GSA-QSRAR--------------EAEkQLREQVGDQYQTVRA----LAER----KAEGVLAAQARAEQLRDEARDLLQAA 1746
Cdd:NF041483 644 ADAsAARAEgenvavrlrseaaaEAE-RLKSEAQESADRVRAeaaaAAERvgteAAEALAAAQEEAARRRREAEETLGSA 722
|
330 340
....*....|....*....|.
gi 31982223 1747 QDKLQrlQELEGTYEENERAL 1767
Cdd:NF041483 723 RAEAD--QERERAREQSEELL 741
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1144-1191 |
1.50e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 31982223 1144 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1191
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1444-1768 |
4.55e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.31 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1444 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1519
Cdd:NF041483 720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1520 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAHRARSRA 1598
Cdd:NF041483 787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1599 EGERQKAE-----TVQAALEEAQR----AQGAAQGAIWGAVVDTQNTEQTLQRVQ-ERMAGAEKSLNSAGERARQL--DA 1666
Cdd:NF041483 843 QEETEAAKalaerTVSEAIAEAERlrsdASEYAQRVRTEASDTLASAEQDAARTRaDAREDANRIRSDAAAQADRLigEA 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1667 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAA 1746
Cdd:NF041483 923 TSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002
|
330 340
....*....|....*....|..
gi 31982223 1747 QDKLQRLQelEGTYEENERALE 1768
Cdd:NF041483 1003 AAEAERLR--TEAREEADRTLD 1022
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1461-1757 |
5.75e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 67.47 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1461 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1519
Cdd:pfam07111 354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1520 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRRAEQLLQ-DAH----- 1592
Cdd:pfam07111 434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRLDAELQlSAHliqqe 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1593 --RARSRAEGERQKAETVqaaleeaqraqgaaqgaiwgavvdTQNTEQTLQRVQERMAGAEKSLNSAgeRARQLDALLEA 1670
Cdd:pfam07111 508 vgRAREQGEAERQQLSEV------------------------AQQLEQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1671 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1734
Cdd:pfam07111 562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633
|
330 340
....*....|....*....|....
gi 31982223 1735 -LRDEARDllQAAQDKLQRLQELE 1757
Cdd:pfam07111 634 rLQDEARK--EEGQRLARRVQELE 655
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1096-1144 |
6.35e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 6.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 1096 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDPGLQCRAC 1144
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
832-880 |
6.74e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 6.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 832 CQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFPNCRPCVC 880
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-565 |
9.53e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 9.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 31982223 524 PCDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFRP 565
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-564 |
9.91e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 9.91e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 31982223 525 CDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFR 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
413-470 |
1.24e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASDPRGC 470
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1143-1192 |
2.17e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.36 E-value: 2.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1143 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1192
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1039-1093 |
2.95e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 2.95e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1039 CTCNLLGTDPRrcpstdlcHCDPSTGQCPCLPHVQGLNCDHCAPNFWNF--TSGRGC 1093
Cdd:pfam00053 1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1554-1779 |
3.28e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 65.62 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1554 QRLASEIAERVRsladvdTILAHTMGDVRRAEQLlqdahRAR-----------SRAEGERQ----KAETVQAALEEAQRA 1618
Cdd:NF041483 130 QQLDQELAERRQ------TVESHVNENVAWAEQL-----RARtesqarrlldeSRAEAEQAlaaaRAEAERLAEEARQRL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1619 QGAAQGAIWGAvvdtqntEQTLQRVQermAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAA-STAEETAGSAQSRAR 1697
Cdd:NF041483 199 GSEAESARAEA-------EAILRRAR---KDAERLLNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQRMQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1698 EAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDllQAAQDKLQRLQELEGTYEENERALEGKAAQLDGL 1777
Cdd:NF041483 269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKE--EIARLVGEATKEAEALKAEAEQALADARAEAEKL 346
|
..
gi 31982223 1778 EA 1779
Cdd:NF041483 347 VA 348
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1456-1762 |
4.02e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 65.23 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1456 RARHTQAELQRALVEgggilSRVSETRRQAE-------EAQQRAQAALDKANASRGQveQANQELRELIQNVKDFLSQEG 1528
Cdd:NF041483 79 RNAQIQADQLRADAE-----RELRDARAQTQrilqehaEHQARLQAELHTEAVQRRQ--QLDQELAERRQTVESHVNENV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1529 ADPDSI----EMVATRVLDIS-------IPASPEQIQRLASEIAERVRSLADVdtilAHTmgdvrRAEQLLQdahraRSR 1597
Cdd:NF041483 152 AWAEQLrartESQARRLLDESraeaeqaLAAARAEAERLAEEARQRLGSEAES----ARA-----EAEAILR-----RAR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1598 AEGERqkaeTVQAALEEAQRAQGAAQGAiwgAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQldALLEALKLkrag 1677
Cdd:NF041483 218 KDAER----LLNAASTQAQEATDHAEQL---RSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE--ARAEAEKV---- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1678 nslaASTAEETAG----SAQS----RAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDEARDLLQ--AA 1746
Cdd:NF041483 285 ----VAEAKEAAAkqlaSAESaneqRTRTAKEEIARLVGEATKEAEALKA-EAEQALAdARAEAEKLVAEAAEKARtvAA 359
|
330
....*....|....*.
gi 31982223 1747 QDKLQRLQELEGTYEE 1762
Cdd:NF041483 360 EDTAAQLAKAARTAEE 375
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1144-1188 |
6.74e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 6.74e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 1144 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1188
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1444-1788 |
1.21e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.69 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1444 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1522
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1523 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1589
Cdd:NF041483 984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1590 DAHRA--RSRAEGERQKAETVQAALEEAQRAQGAAqgaiwgAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDAL 1667
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERIVAEA------TVEGNSLVEKARTDADELLVGARRDATAIRERAEELRDR 1129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1668 LE--------------ALKLKRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AAQ 1729
Cdd:NF041483 1130 ITgeieelherarresAEQMKSAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAEQ 1205
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1730 ARAEQLRdeardllQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEA---RMRSVLQAI 1788
Cdd:NF041483 1206 KKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1038-1094 |
1.35e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.35e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1038 RCTCNLLGTDPRRCpstdlchcDPSTGQCPCLPHVQGLNCDHCAPNFWNFTS-GRGCQ 1094
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
473-527 |
1.47e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 1.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 473 CQCNSRGTVpgSSPCDSSSGTCFCKRLVTGHGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1096-1141 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 1.79e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 1096 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDPGLQC 1141
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-523 |
2.36e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 2.36e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 31982223 472 RCQCNSRGTVPGSspCDSSSGTCFCKRLVTGHGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1095-1142 |
2.68e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.28 E-value: 2.68e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1095 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDP--GLQCR 1142
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
412-471 |
3.10e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.28 E-value: 3.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASDPRGCQ 471
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
831-873 |
5.86e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.51 E-value: 5.86e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 31982223 831 ACQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFP 873
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
832-873 |
9.28e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 9.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 31982223 832 CQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFP 873
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1039-1093 |
1.01e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1039 CTCNLLGTDPRrcpstdlcHCDPSTGQCPCLPHVQGLNCDHCAPNFWNFtSGRGC 1093
Cdd:smart00180 1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
525-564 |
1.09e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.09e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 31982223 525 CDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFR 564
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
987-1029 |
2.85e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 2.85e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 31982223 987 CECSGNIDPmdPDACDPHTGQCLrCLHNTEGPHCGYCKPGFHG 1029
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
413-466 |
1.17e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 1.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 31982223 413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASD 466
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1787 |
1.32e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 56.76 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAEL---------QRALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasRGQVEQANQELREL 1516
Cdd:NF041483 277 ARAEAEKVVAEAKEAAAKQlasaesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADA---RAEAEKLVAEAAEK 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1517 IQNV--KDFLSQEGADPDSIEMVATRVLD---ISIPASPEQIQRL--------------ASEIAERVRSLADVDT--ILA 1575
Cdd:NF041483 354 ARTVaaEDTAAQLAKAARTAEEVLTKASEdakATTRAAAEEAERIrreaeaeadrlrgeAADQAEQLKGAAKDDTkeYRA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1576 HTM---GDVRR----AEQLlqdahRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTlqrvqermA 1648
Cdd:NF041483 434 KTVelqEEARRlrgeAEQL-----RAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRST--------A 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1649 GAEkslnsaGERARQlDALLEALKLKRagnslaasTAEETAgsaqSRAREAEKQLREQVGDQYQTVRALAERKAE----- 1723
Cdd:NF041483 501 TAE------SERVRT-EAIERATTLRR--------QAEETL----ERTRAEAERLRAEAEEQAEEVRAAAERAARelree 561
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1724 ---GVLAAQARA----EQLRDEARDLLQAAQdklqrlQELEGTYEENERALEGKAAQLDGLEA----RMRSvLQA 1787
Cdd:NF041483 562 terAIAARQAEAaeelTRLHTEAEERLTAAE------EALADARAEAERIRREAAEETERLRTeaaeRIRT-LQA 629
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1204-1571 |
1.66e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1204 DLAARTRRLEQWAQELQQTgvLGAFESSFLNMQGKLGMVQAIMSARNASAASTAKLVEAtegLRHEIGKTTERLTQLEAE 1283
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA--LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR---LEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1284 LTAVQDENFNANHALSGLERDGLALNLTLRQLDQhlEILKHSNFLGAYDS-IRHAHSQSTEAERRANASTFAVPSPVSNS 1362
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEA--QIEQLKEELKALREaLDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1363 ADTRRRTEVLmgaqkenfnrqhlanQQALGRLSAHAhtLSLTG-INELvcgapgdapcatspcggagcrdedgqprcggl 1441
Cdd:TIGR02168 834 AATERRLEDL---------------EEQIEELSEDI--ESLAAeIEEL-------------------------------- 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1442 GCSGAAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVK 1521
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1522 DFLSQEGAdpDSIEMVATRVLDisIPASPEQIQRLASEIAERVRSLADVD 1571
Cdd:TIGR02168 943 ERLSEEYS--LTLEEAEALENK--IEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
987-1033 |
2.84e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 2.84e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 31982223 987 CECSGNIDPmdPDACDPHTGQCLrCLHNTEGPHCGYCKPGFHGQAAR 1033
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-516 |
3.35e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 31982223 473 CQCNSRGTVPGSspCDSSSGTCFCKRLVTGHGCDRCLPGHWGLS 516
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
878-925 |
4.02e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 4.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 31982223 878 CVCNGRA---DECDTHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 925
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
877-922 |
6.59e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 6.59e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 877 PCVCNGRAD---ECDTHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 922
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
927-985 |
1.72e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 1.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 31982223 927 PCPCPeGPGSQRHfatSCHRDGYsqqiVCQCREGYTGLRCEACAPGHFGDPSKPGGrCQ 985
Cdd:cd00055 1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
954-984 |
1.25e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.88 E-value: 1.25e-05
10 20 30
....*....|....*....|....*....|.
gi 31982223 954 VCQCREGYTGLRCEACAPGHFGDPSKPGGRC 984
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1446-1745 |
1.26e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.82 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLAlgrarhTQAELQRALVEGggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1525
Cdd:smart00283 17 AEELEELA------ERMEELSASIEE--VAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 QEgadpDSIEMVATRVLDISipaspEQIQRLA-----------------SEIAERVRSLADvdtilahtmgdvrraeqll 1588
Cdd:smart00283 89 SS----DEIGEIVSVIDDIA-----DQTNLLAlnaaieaarageagrgfAVVADEVRKLAE------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1589 qdahraRSRAEgerqkAETVQAALEEAQRAQGAAQGAIWGAvvdTQNTEQTLQRVQErmagAEKSLNSAGERARQLDALL 1668
Cdd:smart00283 141 ------RSAES-----AKEIESLIKEIQEETNEAVAAMEES---SSEVEEGVELVEE----TGDALEEIVDSVEEIADLV 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1669 EalklkragnSLAASTAEETAGSaqsrareaekqlrEQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQA 1745
Cdd:smart00283 203 Q---------EIAAATDEQAAGS-------------EEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
987-1029 |
1.60e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.45 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 31982223 987 CECS--GNIDPmdpdACDPHTGQCLrCLHNTEGPHCGYCKPGFHG 1029
Cdd:smart00180 1 CDCDpgGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-338 |
1.93e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.50 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
928-977 |
2.74e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 2.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 928 CPCPEGpgsqRHFATSCHRDGYsqqiVCQCREGYTGLRCEACAPGHFGDP 977
Cdd:smart00180 1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
350-401 |
3.14e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.73 E-value: 3.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 350 CECNGH---THSCHFdmavylasgnvSGGVCDgCQHNTAGRHCEFCRPFFYRDPT 401
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
350-402 |
3.87e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 42.73 E-value: 3.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 350 CECNGH---THSCHFDmavylasgnvsGGVCDgCQHNTAGRHCEFCRPFFYRDPTK 402
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1697-1793 |
1.25e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1697 REAEKQL---REQVGDQyQTVRALAERKAEgvlAAQARAEQLRDEARDLLQAAQDKL-----QRLQELEGTYEENERALE 1768
Cdd:COG1842 33 RDMEEDLveaRQALAQV-IANQKRLERQLE---ELEAEAEKWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA 108
|
90 100
....*....|....*....|....*
gi 31982223 1769 gkaaQLDGLEARMRSVLQAINLQVQ 1793
Cdd:COG1842 109 ----QLEEQVEKLKEALRQLESKLE 129
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1682-1793 |
1.62e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 44.16 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1682 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARDLLQAAQDKLQRLQELE 1757
Cdd:PRK14475 36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 31982223 1758 GTYEENERALEGKAAQLDgLEARMRSVLQAINLQVQ 1793
Cdd:PRK14475 115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1718-1794 |
4.03e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 42.30 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1718 AERKAEGVLAAQARAEQL----RDEARDLLQAAQDKLQRL-QELEG-TYEENERALEGKAAQLDGLEARMRSVL--QAIN 1789
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121
|
....*
gi 31982223 1790 LQVQI 1794
Cdd:pfam00430 122 LAVQI 126
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
1578-1752 |
4.21e-04 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 45.29 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1578 MGDVRRAEQLLQDAHRARSRAEGERQKAeTVQAA--LEEAQRAQGAAQGAiwgavVDTQntEQTLQRVQERMAG------ 1649
Cdd:NF040586 533 LGDYREALELDREVLRRRRRVLGPDHPR-TLLSAnnLARDLRELGRYAEA-----LDLL--EEALERYREVLGGpdhpdt 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1650 --AEKSLNSAgerARQLDALLEALKLKR-------------------AGNSLAA--STAEETAGsAQSRAREAEKQLREQ 1706
Cdd:NF040586 605 lrAAKSLAVA---LRRAGRLEEALELAEdtyeryrrrfgpdhpdtlaAALSLANdlRALGDADE-ARELAREVLDRYRRV 680
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31982223 1707 VGDQYQTVRAlaerkAEGVLAAQARAEQLRDEARDLLQAAQDKLQR 1752
Cdd:NF040586 681 LGEDHPFTLA-----CRNNLAVLLRALGDPEEARELAEAALEGLRE 721
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
878-917 |
4.75e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 4.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 31982223 878 CVCNGR---ADECDTHTGACLgCRDYTGGEHCERCIAGFHGDP 917
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1203-1462 |
1.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1203 QDLAARTRRLEQWAQELQQTG--------VLGAfeSSFLNMQGKLGMVQAIMSARNASAASTAKLVEATEGLRHEIGKTT 1274
Cdd:COG3883 79 AEIEERREELGERARALYRSGgsvsyldvLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1275 ERLTQLEAELTAVQDEnfnANHALSglERDGLALNLTLRQLDQHLEILKHSNFLGAYDSIRHAHSQSTEAERRANASTFA 1354
Cdd:COG3883 157 AELEALKAELEAAKAE---LEAQQA--EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1355 VPSPVSNSADTRRrtevlMGAQKENFNRQHLANQQALGRLSAHAHTLSLTGINELVCGAPGDAPCATSPCGGAGCRDEDG 1434
Cdd:COG3883 232 AAAAAAAAAAAAA-----SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGG 306
|
250 260
....*....|....*....|....*...
gi 31982223 1435 QPRCGGLGCSGAAATADLALGRARHTQA 1462
Cdd:COG3883 307 SGGAGGVGSGGGAGAVVGGASAGGGGGS 334
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1637-1782 |
2.71e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 41.19 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1637 EQTLQRVQ---ERMAGAEKSLNSA----GERARQLDALLE--ALKLKRAGNSLAaSTAEETAGSAQSRAREAEKQLREQV 1707
Cdd:cd07596 17 EEQLKKLSkqaQRLVKRRRELGSAlgefGKALIKLAKCEEevGGELGEALSKLG-KAAEELSSLSEAQANQELVKLLEPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1708 GDQYQTVRA----LAERKAEG--VLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARM 1781
Cdd:cd07596 96 KEYLRYCQAvketLDDRADALltLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERL 175
|
.
gi 31982223 1782 R 1782
Cdd:cd07596 176 K 176
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1583-1618 |
2.98e-03 |
|
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.
Pssm-ID: 468572 [Multi-domain] Cd Length: 90 Bit Score: 38.43 E-value: 2.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 31982223 1583 RAEQLLQDAHRARSRAEGERQKAE----TVQAALEEAQRA 1618
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
309-341 |
3.39e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.33 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|...
gi 31982223 309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
350-403 |
3.76e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 350 CECNG---HTHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCEFCRPFFYRDPTKD 403
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-284 |
1.40e-105 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 336.48 E-value: 1.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055 72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 31982223 283 RG 284
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
44-284 |
2.69e-84 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 276.16 E-value: 2.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWHVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136 151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 31982223 277 LYELVIRG 284
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1728-1799 |
2.48e-38 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 137.96 E-value: 2.48e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1728 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1799
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1729-1798 |
3.60e-26 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 103.13 E-value: 3.60e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1729 QARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTC 1798
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1728-1798 |
2.71e-23 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 94.85 E-value: 2.71e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1728 AQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTC 1798
Cdd:cd22300 2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1446-1787 |
7.95e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1525
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKA 1605
Cdd:COG1196 320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1606 ETVQAALEEAQRAQGAAQgaiwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRagnsLAASTA 1685
Cdd:COG1196 378 EEELEELAEELLEALRAA----------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1686 EETAGSAQSRAREAEKQLREQVGDQyQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGtyEENER 1765
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLR 520
|
330 340
....*....|....*....|..
gi 31982223 1766 ALEGKAAQLDGLEARMRSVLQA 1787
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEA 542
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1552-1788 |
4.09e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1552 QIQRLA--SEIAERVRSLADVDTILAHTM---------GDVRRAEQLLQDAHRARSRAEGERQKAET----VQAALEEAQ 1616
Cdd:COG1196 201 QLEPLErqAEKAERYRELKEELKELEAELlllklreleAELEELEAELEELEAELEELEAELAELEAeleeLRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1617 RAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRA 1696
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1697 REAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDG 1776
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250
....*....|..
gi 31982223 1777 LEARMRSVLQAI 1788
Cdd:COG1196 440 EEEALEEAAEEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1275-1793 |
2.45e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1275 ERLTQLEAELTAVQDENFNANHALSGLERDGL-----ALNLTLRQLDQHLEILKHsnflgAYDSIRHAHSQSTEAERRAN 1349
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELeaeleELEAELAELEAELEELRL-----ELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1350 AStfavpspVSNSADTRRRTEVLMGAQKENFNRQHLANQQALGRLSAHAHTLSLtginelvcgapgdapcatspcggagc 1429
Cdd:COG1196 295 AE-------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE-------------------------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1430 rdedgqprcgglgcsgAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQA 1509
Cdd:COG1196 342 ----------------LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1510 NQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASpEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQ 1589
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1590 DAHRARSRAEGERQKAETVQAALEEAQRAQG-AAQGAIWGAVVDTQNTEQTLQRVQERMAGAEkSLNSAGERARQLDALL 1668
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1669 EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQD 1748
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 31982223 1749 KLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQ 1793
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1463-1788 |
2.88e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.09 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1463 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1534
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1535 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAHRARSRAEGERQKAE 1606
Cdd:PRK02224 290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1607 TVQAALEEAQRAQGAAQGAI--------------WGAVVDTQNTE-------QTLQRVQERMAGAEKSLNSAGERARQLD 1665
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIeeleeeieelrerfGDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1666 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1712
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1713 TVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEaRMRSVLQAI 1788
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1197-1789 |
5.17e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1197 DWDRVVQDLAARTRRLEQWAQELQQT-GVLGAFESSFLNMQGKLGMVQAIMSARNASAASTAKLVEATEGLRHEIGKTTE 1275
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELeAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1276 RLTQLEAELTAVQDEnfnANHALSGLERDGLALNLTLRQLDQHLEILKHSnfLGAYDSIRHAHSQSTEAERRANAStfav 1355
Cdd:COG1196 320 ELEEELAELEEELEE---LEEELEELEEELEEAEEELEEAEAELAEAEEA--LLEAEAELAEAEEELEELAEELLE---- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1356 psPVSNSADTRRRTEVLMGAQKENFNRQHLANQQALGRLSAHAHTLSLtginelvcgapgdapcatspcggagcRDEDGQ 1435
Cdd:COG1196 391 --ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------------------------EEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1436 prcgglgcsgAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRE 1515
Cdd:COG1196 443 ----------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1516 LIQNVKDF-LSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVD-----TILAHTMGDVRRAEQLLQ 1589
Cdd:COG1196 513 ALLLAGLRgLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1590 DA---HRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMA----------GAEKSLNS 1656
Cdd:COG1196 593 ARgaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltgGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1657 AGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAAQA 1730
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleellEEEELLEEEA 752
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1731 RAEQLRDEARDLLQAAQDKLQR------------LQELEgtyEENERaLEGKAAQLDGLEARMRSVLQAIN 1789
Cdd:COG1196 753 LEELPEPPDLEELERELERLEReiealgpvnllaIEEYE---ELEER-YDFLSEQREDLEEARETLEEAIE 819
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1446-1782 |
6.09e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.94 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAAT---ADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEqanqELRELIQNVKD 1522
Cdd:PRK02224 232 ARETrdeADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDL-------RERLE----ELEEERDDLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1523 FLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAHRARSRAEGER 1602
Cdd:PRK02224 301 EAGLDDADAEAVE---------------ARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1603 QKAETVQAALEEAQRAQGAAQGAI--------------WGAVVDTQNTE-------QTLQRVQERMAGAEKSLNSAGERA 1661
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIeeleeeieelrerfGDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1662 RQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLrEQVGDQYQTVRALAERkAEGVLAAQARAEQLRDEARD 1741
Cdd:PRK02224 443 EEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAEL-EDLEEEVEEVEERLER-AEDLVEAEDRIERLEERRED 520
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 31982223 1742 LlqaaqdkLQRLQELEGTYEENERALEGKAAQLDGLEARMR 1782
Cdd:PRK02224 521 L-------EELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1562-1786 |
1.96e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.66 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1562 ERVRSLADVDTILAHtMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGA-IWGAVVDTQNTEQTL 1640
Cdd:COG4913 219 EEPDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1641 QRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQT-VRAL-- 1717
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----REIERLERELEERERRRARLEAlLAALgl 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1718 -AERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLqelegtyeenERALEGKAAQLDGLEARMRSVLQ 1786
Cdd:COG4913 374 pLPASAEEFAALRAEAAALLEALEEELEALEEALAEA----------EAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1472-1794 |
9.75e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.49 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1472 GGILSR---VSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsQEGADPDSIEMVATRvldISIPA 1548
Cdd:TIGR02168 670 SSILERrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQISALR---KDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1549 SPEQIQRLASEIAERVRSLADVDtilAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIwg 1628
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-- 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1629 avvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAgnSLAASTAEEtagsaQSRAREAEKQLrEQVG 1708
Cdd:TIGR02168 813 -----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE--SLAAEIEEL-----EELIEELESEL-EALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1709 DQYQTVRALAERkaegvlaAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQaI 1788
Cdd:TIGR02168 880 NERASLEEALAL-------LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-L 951
|
....*.
gi 31982223 1789 NLQVQI 1794
Cdd:TIGR02168 952 TLEEAE 957
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1729-1798 |
1.19e-14 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 70.34 E-value: 1.19e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1729 QARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTC 1798
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1457-1788 |
2.45e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1457 ARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASR----GQVEQANQELRELIQNVKDFlsQEGADPD 1532
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEEL--EAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1533 SIEMVATRvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAEtvqAAL 1612
Cdd:TIGR02168 795 KEELKALR----------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---AEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1613 EEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAgnslaasTAEETAGSA 1692
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-------QLELRLEGL 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1693 QSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDL-------LQAAQDKLQRLQELEGTYEENER 1765
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTE 1014
|
330 340
....*....|....*....|...
gi 31982223 1766 ALEGKAAQLDGLEARMRSVLQAI 1788
Cdd:TIGR02168 1015 AKETLEEAIEEIDREARERFKDT 1037
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
784-829 |
1.13e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.57 E-value: 1.13e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 784 CQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGFGPAGC 829
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
784-832 |
1.32e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 1.32e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 784 CQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGFGPAGCQAC 832
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
783-830 |
1.83e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 1.83e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 783 PCQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGF--GPAGCQ 830
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1574-1788 |
4.71e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1574 LAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWgavvdtQNTEQTLQRVQERMAGAEKS 1653
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKL------RELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1654 LNSAGERARQLDALLEALKLKRagnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAE 1733
Cdd:COG1196 255 LEELEAELAELEAELEELRLEL-----------EELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1734 QLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAI 1788
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1447-1794 |
7.76e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 74.22 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1447 AATADLALGRARHtQAELQRALVEGGGILSRVSETRRQAEEAQQRA---QAALDKANASRGQVEQANQELRELIQNVKDF 1523
Cdd:PRK04863 265 ESTNYVAADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1524 LSQEGAdpdsIEMVATRVLDISIPA-SPEQIQRLASEIAERVRSLA-----DVDTiLAHTMGDVRRAEQLLQdahrarSR 1597
Cdd:PRK04863 344 LRQQEK----IERYQADLEELEERLeEQNEVVEEADEQQEENEARAeaaeeEVDE-LKSQLADYQQALDVQQ------TR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1598 AeGERQKAetvQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKlkRAG 1677
Cdd:PRK04863 413 A-IQYQQA---VQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVR--KIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1678 NSLAASTAEETAgsaqsraREAEKQLREQ--VGDQYQTVRA-LAErkAEGVLAAQARAEQLRDEArdlLQAAQDKLQRLQ 1754
Cdd:PRK04863 487 GEVSRSEAWDVA-------RELLRRLREQrhLAEQLQQLRMrLSE--LEQRLRQQQRAERLLAEF---CKRLGKNLDDED 554
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 31982223 1755 ELEGTYEENERALEGKAAQLDGLEARmRSVLQAINLQVQI 1794
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQA 593
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1438-1730 |
1.76e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 71.40 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1438 CGGLGCSGAAATADLALGRARHTQAELQRALVEgggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELI 1517
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1518 QNVKD----------FLSQEGADPDSIEMVATrvldisipaspeqiqrlASEIAERVRSLADVDTILAHTMGDVRRAEQL 1587
Cdd:COG3883 79 AEIEErreelgerarALYRSGGSVSYLDVLLG-----------------SESFSDFLDRLSALSKIADADADLLEELKAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1588 LQDAHRARSRAEGERQKAETVQAALEEAQRaqgAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDAL 1667
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31982223 1668 LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQA 1730
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASA 281
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1461-1788 |
2.21e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.68 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1461 QAELQRALVEGGGilSRVSETRRQAEEAQQRA----------QAALDKANASRGQVEQANQELRE----------LIQNV 1520
Cdd:PRK04863 363 RLEEQNEVVEEAD--EQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1521 KDFLSQEGADPDSiemVATRVLDIsipaspEQIQRLASEIAER-------VRSLAD-VDTILAHtmgdvRRAEQLLQDAH 1592
Cdd:PRK04863 441 EDWLEEFQAKEQE---ATEELLSL------EQKLSVAQAAHSQfeqayqlVRKIAGeVSRSEAW-----DVARELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1593 RARSRAegerQKAETVQAALEEAQRaqgaaqgaiwgavvdtQNTEQtlQRVQERMAGAEKSLNSAGERARQLDALLEALK 1672
Cdd:PRK04863 507 EQRHLA----EQLQQLRMRLSELEQ----------------RLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1673 LKRAGNSLAASTAEETagsaqsraREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQLRDEARDLLQAAQDKLQR 1752
Cdd:PRK04863 565 ARLESLSESVSEARER--------RMALRQQLEQLQARIQRLAARAPA----WLAAQDALARLREQSGEEFEDSQDVTEY 632
|
330 340 350
....*....|....*....|....*....|....*.
gi 31982223 1753 LQELegtyEENERALEgkaAQLDGLEARMRSVLQAI 1788
Cdd:PRK04863 633 MQQL----LERERELT---VERDELAARKQALDEEI 661
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1490-1792 |
3.54e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 71.59 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1490 QRAQAALDKANASRGQVEQANQELRELIQNVKdflsqegadpdsIEMVA-TRVLDISIPA-SPEQIQRLASEIAErvrsl 1567
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLT------------VEPVKgSNVIEISYTSpDPELAAAVANALAE----- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1568 ADVDTILAHTMGDVRRAEQLLQDahrarsRAEGERQKAETVQAALEEAQRAQGaaqgaiwgaVVDTQNTEQTLQrvqERM 1647
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNG---------LVDLSEEAKLLL---QQL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1648 AGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE-----KQLREQVGDQYQTVRALAERKA 1722
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEleaelAELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1723 E----------GVLAA---------------QARAEQLRDEARDLlqaaQDKLQRLQELEGTYEENERALEGKAAQLDgl 1777
Cdd:COG3206 302 AlraqlqqeaqRILASleaelealqareaslQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLE-- 375
|
330
....*....|....*
gi 31982223 1778 EARMRSVLQAINLQV 1792
Cdd:COG3206 376 EARLAEALTVGNVRV 390
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1551-1789 |
3.79e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIAERVRS------------LADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEaqra 1618
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKdlherlngleseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1619 qgaaqgaiwgavvdtqnteqtlqrVQERMAGAEKSLNSAGERARQLDALLEALKLKRAG--NSLAASTAEETAGSAQSRA 1696
Cdd:PRK02224 263 ------------------------LRETIAETEREREELAEEVRDLRERLEELEEERDDllAEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1697 REAEK-QLREQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARDL---LQAAQDKLQ----RLQELEGTYEENER 1765
Cdd:PRK02224 319 LEDRDeELRDRLEECRVAAQAHneeAESLREDADDLEERAEELREEAAELeseLEEAREAVEdrreEIEELEEEIEELRE 398
|
250 260
....*....|....*....|....
gi 31982223 1766 ALEGKAAQLDGLEARMRSVLQAIN 1789
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1456-1789 |
4.21e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1456 RARHTQAELQRALVEGG-GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDF-LSQEGADPDS 1533
Cdd:COG4717 171 ELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAaLEERLKEARL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1534 IEMVATRVLDISIPASpeQIQRLASEIAERVRSLAdvdTILAHTMGDVRRAEQLLQdahRARSRAEGERQKAETVQAALE 1613
Cdd:COG4717 251 LLLIAAALLALLGLGG--SLLSLILTIAGVLFLVL---GLLALLFLLLAREKASLG---KEAEELQALPALEELEEEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1614 EAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAgERARQLDALLEAlklkragnslAASTAEETAGSAQ 1693
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAE----------AGVEDEEELRAAL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1694 SRAREAEK------QLREQVGDQYQTVRALAERKAEGVLAAQ-ARAEQLRDEARDLLQAAQDKL----QRLQELE--GTY 1760
Cdd:COG4717 392 EQAEEYQElkeeleELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELaeleAELEQLEedGEL 471
|
330 340 350
....*....|....*....|....*....|..
gi 31982223 1761 EENERALEGKAAQLDGLE---ARMRSVLQAIN 1789
Cdd:COG4717 472 AELLQELEELKAELRELAeewAALKLALELLE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1448-1777 |
6.01e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1448 ATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALdkaNASRGQVEQANQELRELIQNVKDflsqe 1527
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLAN----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1528 gadpdsiemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEgerQKAET 1607
Cdd:TIGR02168 314 --------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE---SRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1608 VQAALEEAQRAQGAAQGAIwgavvdTQNTEQtLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAE- 1686
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQI------ASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEl 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1687 ETAGSAQSRAREAEKQLREQVgdqyqtvralaerkaegvlaaqARAEQLRDEARDLLQAAQ---DKLQRLQELEGTYEEN 1763
Cdd:TIGR02168 450 EELQEELERLEEALEELREEL----------------------EEAEQALDAAERELAQLQarlDSLERLQENLEGFSEG 507
|
330
....*....|....
gi 31982223 1764 ERALEGKAAQLDGL 1777
Cdd:TIGR02168 508 VKALLKNQSGLSGI 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1463-1796 |
7.31e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 69.16 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1463 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVL 1542
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1543 DISipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQraqgaA 1622
Cdd:COG4372 112 ELQ-----EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE-----A 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1623 QGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNsagERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQ 1702
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPR---ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1703 LREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKlqrLQELEGTYEENERALEGKAAQLDGLEARMR 1782
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA---ALSLIGALEDALLAALLELAKKLELALAIL 335
|
330
....*....|....
gi 31982223 1783 SVLQAINLQVQIYN 1796
Cdd:COG4372 336 LAELADLLQLLLVG 349
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1480-1767 |
1.43e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 69.85 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1480 ETRRQAEEAQQRAQAALDKANASRGQV-EQANQELRELIQNVKDFLSQEGADPDSIEMVATrvldisipaspEQIQRLAS 1558
Cdd:NF041483 441 EARRLRGEAEQLRAEAVAEGERIRGEArREAVQQIEEAARTAEELLTKAKADADELRSTAT-----------AESERVRT 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1559 EIAERVRSLAdvdtilahtmgdvRRAEQLLQdahraRSRAEGERQKAEtvqaALEEAQRAQGAAQGAiwgAVVDTQNTEQ 1638
Cdd:NF041483 510 EAIERATTLR-------------RQAEETLE-----RTRAEAERLRAE----AEEQAEEVRAAAERA---ARELREETER 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1639 T-----------LQRVQ----ERMAGAEKSLNSA---GERARQlDALLEALKLK-------RAGNSLAASTAE----ETA 1689
Cdd:NF041483 565 AiaarqaeaaeeLTRLHteaeERLTAAEEALADAraeAERIRR-EAAEETERLRteaaeriRTLQAQAEQEAErlrtEAA 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1690 GSA-QSRAR--------------EAEkQLREQVGDQYQTVRA----LAER----KAEGVLAAQARAEQLRDEARDLLQAA 1746
Cdd:NF041483 644 ADAsAARAEgenvavrlrseaaaEAE-RLKSEAQESADRVRAeaaaAAERvgteAAEALAAAQEEAARRRREAEETLGSA 722
|
330 340
....*....|....*....|.
gi 31982223 1747 QDKLQrlQELEGTYEENERAL 1767
Cdd:NF041483 723 RAEAD--QERERAREQSEELL 741
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1144-1191 |
1.50e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 31982223 1144 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1191
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1466-1796 |
1.64e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1466 RALVE-GGGIlSRVSETRRQAEEAQQRAQAALDKANASRG-----------QVEQAnQELRELiqnvKDFLSQegadpds 1533
Cdd:TIGR02168 158 RAIFEeAAGI-SKYKERRKETERKLERTRENLDRLEDILNelerqlkslerQAEKA-ERYKEL----KAELRE------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1534 iemvatrvLDISIpaspeqiqrLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAEtvqAALE 1613
Cdd:TIGR02168 225 --------LELAL---------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE---EEIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1614 EAQRAQGAAQGAIwgavvdtQNTEQTLQRVQERMAGAEKS--------------LNSAGERARQLDALLEALKLKRAGNS 1679
Cdd:TIGR02168 285 ELQKELYALANEI-------SRLEQQKQILRERLANLERQleeleaqleeleskLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1680 LAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLA------AQARAEQLRDEARDLLQAAQDklQRL 1753
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLearlerLEDRRERLQQEIEELLKKLEE--AEL 435
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 31982223 1754 QELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYN 1796
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1456-1773 |
2.73e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1456 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE 1535
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1536 mVATRVLDisipASPEQIQRLASEI--AERVRSLADVDTI-LAHTMGDVRRAEQlLQDAHRARsRAEgERQKAETVQAAL 1612
Cdd:PTZ00121 1168 -EARKAED----AKKAEAARKAEEVrkAEELRKAEDARKAeAARKAEEERKAEE-ARKAEDAK-KAE-AVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1613 EEAQRAQgaaqgaiwgavvDTQNTEQTLQRVQERMAG-AEKSLNSAGERARQLDALLEALKLKRAgNSLAASTAEETAGS 1691
Cdd:PTZ00121 1240 EEAKKAE------------EERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAEEKKKA-DEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1692 AQSRAREAEK--QLREQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARDLLQAAQ-DKLQRLQELEGTYEENER 1765
Cdd:PTZ00121 1307 AKKKAEEAKKadEAKKKAEEAKKKADAAkkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKK 1386
|
....*...
gi 31982223 1766 ALEGKAAQ 1773
Cdd:PTZ00121 1387 AEEKKKAD 1394
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1444-1768 |
4.55e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.31 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1444 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1519
Cdd:NF041483 720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1520 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAHRARSRA 1598
Cdd:NF041483 787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1599 EGERQKAE-----TVQAALEEAQR----AQGAAQGAIWGAVVDTQNTEQTLQRVQ-ERMAGAEKSLNSAGERARQL--DA 1666
Cdd:NF041483 843 QEETEAAKalaerTVSEAIAEAERlrsdASEYAQRVRTEASDTLASAEQDAARTRaDAREDANRIRSDAAAQADRLigEA 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1667 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAA 1746
Cdd:NF041483 923 TSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002
|
330 340
....*....|....*....|..
gi 31982223 1747 QDKLQRLQelEGTYEENERALE 1768
Cdd:NF041483 1003 AAEAERLR--TEAREEADRTLD 1022
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1461-1757 |
5.75e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 67.47 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1461 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1519
Cdd:pfam07111 354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1520 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRRAEQLLQ-DAH----- 1592
Cdd:pfam07111 434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRLDAELQlSAHliqqe 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1593 --RARSRAEGERQKAETVqaaleeaqraqgaaqgaiwgavvdTQNTEQTLQRVQERMAGAEKSLNSAgeRARQLDALLEA 1670
Cdd:pfam07111 508 vgRAREQGEAERQQLSEV------------------------AQQLEQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1671 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1734
Cdd:pfam07111 562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633
|
330 340
....*....|....*....|....
gi 31982223 1735 -LRDEARDllQAAQDKLQRLQELE 1757
Cdd:pfam07111 634 rLQDEARK--EEGQRLARRVQELE 655
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1453-1788 |
5.92e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.06 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1453 ALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA--------------QAALDKANASRGQVEQANQELREliq 1518
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAeeevdslksqladyQQALDVQQTRAIQYQQAVQALEK--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1519 nvkdflSQE--GADPDSIEMVATRVldisipaspEQIQRLASEIAERVRSLadvdtilahtmgdvrraEQLLQDAHRARS 1596
Cdd:COG3096 425 ------ARAlcGLPDLTPENAEDYL---------AAFRAKEQQATEEVLEL-----------------EQKLSVADAARR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1597 R------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERA 1661
Cdd:COG3096 473 QfekayelvckiaGEVERSQAwQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1662 RQLDALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGDQYQTVRAlaerKAEGVLAAQARAEQLRDEARD 1741
Cdd:COG3096 553 EELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQL-EQLRARIKELAA----RAPAWLAAQDALERLREQSGE 620
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 31982223 1742 LLQAAQDKLQRLQELegtyEENERALEgkaAQLDGLEARMRSVLQAI 1788
Cdd:COG3096 621 ALADSQEVTAAMQQL----LEREREAT---VERDELAARKQALESQI 660
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1096-1144 |
6.35e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 6.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 1096 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDPGLQCRAC 1144
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
832-880 |
6.74e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 6.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 832 CQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFPNCRPCVC 880
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1211-1768 |
8.87e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.17 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1211 RLEQWAQELQQtgvlgaFESSFLNMQGKLGmvqAIMSARNASAASTAKLVEATEGLRHEIGKTTERLTQLEAELT---AV 1287
Cdd:pfam12128 242 EFTKLQQEFNT------LESAELRLSHLHF---GYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgelSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1288 QDENF-NANHALSGLERDGLA-LNLTLRQLDQHLEIL------------KHSNFLGAYDSIrhahSQSTEAeRRANASTf 1353
Cdd:pfam12128 313 ADAAVaKDRSELEALEDQHGAfLDADIETAAADQEQLpswqselenleeRLKALTGKHQDV----TAKYNR-RRSKIKE- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1354 avpSPVSNSADTRRRTEvlmgAQKENFNRQHLANQQALGRLSA---HAHTLSLTGINE---LVCGAPG------DAPCAT 1421
Cdd:pfam12128 387 ---QNNRDIAGIKDKLA----KIREARDRQLAVAEDDLQALESelrEQLEAGKLEFNEeeyRLKSRLGelklrlNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1422 SpcggagcrDEDGQPRCGGLGCSgaaaTADLALGRARHTQAELQRALvegggilsRVSETRR-QAEEAQQRAQAALDkan 1500
Cdd:pfam12128 460 P--------ELLLQLENFDERIE----RAREEQEAANAEVERLQSEL--------RQARKRRdQASEALRQASRRLE--- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1501 asrgQVEQANQELRELI----QNVKDFLSQEGAD-PDSIEMVATRVL----DI---SIPASPEQIQRLASeIAERVRSLa 1568
Cdd:pfam12128 517 ----ERQSALDELELQLfpqaGTLLHFLRKEAPDwEQSIGKVISPELlhrtDLdpeVWDGSVGGELNLYG-VKLDLKRI- 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1569 DVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQ---NTEQTLQRVQE 1645
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRrlfDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1646 RMAGAEKslNSAGERARQLDALLEALKLKRAgnslAAStaEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGV 1725
Cdd:pfam12128 671 KALAERK--DSANERLNSLEAQLKQLDKKHQ----AWL--EEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARR 742
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 31982223 1726 LAAQARAEQLRDE-ARDLLQAAQDKlQRLQELEGTYEENERALE 1768
Cdd:pfam12128 743 SGAKAELKALETWyKRDLASLGVDP-DVIAKLKREIRTLERKIE 785
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-565 |
9.53e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 9.53e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 31982223 524 PCDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFRP 565
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-564 |
9.91e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 9.91e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 31982223 525 CDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFR 564
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
413-470 |
1.24e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 1.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASDPRGC 470
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1730-1799 |
1.49e-10 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 58.61 E-value: 1.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1730 ARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1799
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1773 |
1.80e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1477 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLdisipASPEQIQRl 1556
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL-----KKAEEKKK- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1557 ASEI--AERVRSLADvdtiLAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALE----EAQRAQGAAQGAIWGAV 1630
Cdd:PTZ00121 1292 ADEAkkAEEKKKADE----AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakaEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1631 VDTQNTEQ------TLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAAST-----AEETAGSAQS--RAR 1697
Cdd:PTZ00121 1368 AAEKKKEEakkkadAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeekkkADEAKKKAEEakKAD 1447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1698 EAEKQLREQVGDQYQTVRALAERKAEgvlAAQARAEQLRdEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQ 1773
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1547-1794 |
1.98e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1547 PASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQ----KAETVQAALEEAQRAQGAA 1622
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1623 QGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNS-----AGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRar 1697
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE-- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1698 eaEKQLREQVGDQYQTVRALAERKAEgvlaAQARAEQLRDEARDLlqaaqdkLQRLQELEGTYEENERALEGKAAQLDGL 1777
Cdd:TIGR02169 828 --KEYLEKEIQELQEQRIDLKEQIKS----IEKEIENLNGKKEEL-------EEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260
....*....|....*....|
gi 31982223 1778 EARMRSV---LQAINLQVQI 1794
Cdd:TIGR02169 895 EAQLRELerkIEELEAQIEK 914
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1143-1192 |
2.17e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.36 E-value: 2.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1143 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1192
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1446-1793 |
2.23e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAELQRALVEgggiLSRVSETRRQAEEAQQRAQAALDKANASR-----GQVEQANQELRELIQNV 1520
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRleqleREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1521 KDFlsqegadpdsieMVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEG 1600
Cdd:COG4913 362 ARL------------EALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1601 ER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIWG----------------AVVD 1632
Cdd:COG4913 427 EIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltllvppehyaaalRWVN 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1633 TQNTEQTL--QRVQERMAGAEKSLNSAGERARQLD-----------ALL------------EALK-----LKRAG----- 1677
Cdd:COG4913 507 RLHLRGRLvyERVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleAELgrrfdyvcvdspEELRrhpraITRAGqvkgn 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1678 ---------------------NSLAASTAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAERKAE------GVLAA 1728
Cdd:COG4913 587 gtrhekddrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEyswdeiDVASA 666
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1729 QARAEQLRDEaRDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQ 1793
Cdd:COG4913 667 EREIAELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1039-1093 |
2.95e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 2.95e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1039 CTCNLLGTDPRrcpstdlcHCDPSTGQCPCLPHVQGLNCDHCAPNFWNF--TSGRGC 1093
Cdd:pfam00053 1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1554-1779 |
3.28e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 65.62 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1554 QRLASEIAERVRsladvdTILAHTMGDVRRAEQLlqdahRAR-----------SRAEGERQ----KAETVQAALEEAQRA 1618
Cdd:NF041483 130 QQLDQELAERRQ------TVESHVNENVAWAEQL-----RARtesqarrlldeSRAEAEQAlaaaRAEAERLAEEARQRL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1619 QGAAQGAIWGAvvdtqntEQTLQRVQermAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAA-STAEETAGSAQSRAR 1697
Cdd:NF041483 199 GSEAESARAEA-------EAILRRAR---KDAERLLNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQRMQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1698 EAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDllQAAQDKLQRLQELEGTYEENERALEGKAAQLDGL 1777
Cdd:NF041483 269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKE--EIARLVGEATKEAEALKAEAEQALADARAEAEKL 346
|
..
gi 31982223 1778 EA 1779
Cdd:NF041483 347 VA 348
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1441-1697 |
4.01e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1441 LGCSGAAATADlalgRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV 1520
Cdd:COG4942 10 LLALAAAAQAD----AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1521 KDFLSQEGADPDSIE----MVATRVLDISIPASPEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRA 1594
Cdd:COG4942 86 AELEKEIAELRAELEaqkeELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1595 RSRAEGERQKAETVQAALEEAQRAQGAAQgaiwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLK 1674
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|...
gi 31982223 1675 ragnslAASTAEETAGSAQSRAR 1697
Cdd:COG4942 236 ------AAAAAERTPAAGFAALK 252
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1456-1762 |
4.02e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 65.23 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1456 RARHTQAELQRALVEgggilSRVSETRRQAE-------EAQQRAQAALDKANASRGQveQANQELRELIQNVKDFLSQEG 1528
Cdd:NF041483 79 RNAQIQADQLRADAE-----RELRDARAQTQrilqehaEHQARLQAELHTEAVQRRQ--QLDQELAERRQTVESHVNENV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1529 ADPDSI----EMVATRVLDIS-------IPASPEQIQRLASEIAERVRSLADVdtilAHTmgdvrRAEQLLQdahraRSR 1597
Cdd:NF041483 152 AWAEQLrartESQARRLLDESraeaeqaLAAARAEAERLAEEARQRLGSEAES----ARA-----EAEAILR-----RAR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1598 AEGERqkaeTVQAALEEAQRAQGAAQGAiwgAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQldALLEALKLkrag 1677
Cdd:NF041483 218 KDAER----LLNAASTQAQEATDHAEQL---RSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE--ARAEAEKV---- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1678 nslaASTAEETAG----SAQS----RAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDEARDLLQ--AA 1746
Cdd:NF041483 285 ----VAEAKEAAAkqlaSAESaneqRTRTAKEEIARLVGEATKEAEALKA-EAEQALAdARAEAEKLVAEAAEKARtvAA 359
|
330
....*....|....*.
gi 31982223 1747 QDKLQRLQELEGTYEE 1762
Cdd:NF041483 360 EDTAAQLAKAARTAEE 375
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1460-1780 |
4.54e-10 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 63.93 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1460 TQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGADPDSIEMVAT 1539
Cdd:pfam19220 39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE--AEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1540 RvldisipASPEQIQRLASEIAERVRSLADvdtilahtmgDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAq 1619
Cdd:pfam19220 117 T-------AQAEALERQLAAETEQNRALEE----------ENKALREEAQAAEKALQRAEGELATARERLALLEQENRR- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1620 gaaqgaiwgavvdtqnteqtLQRVQERMAgAEksLNSAGERARQLDALLEALklkragnsLAASTAEETAGSAQSRARE- 1698
Cdd:pfam19220 179 --------------------LQALSEEQA-AE--LAELTRRLAELETQLDAT--------RARLRALEGQLAAEQAEREr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1699 AEKQLREQVGdQYQTVRALAERKAEGVLAAQARAEQLRDEARDllqaaqdklqRLQELEGTYEENERALEGKAAQLDGLE 1778
Cdd:pfam19220 228 AEAQLEEAVE-AHRAERASLRMKLEALTARAAATEQLLAEARN----------QLRDRDEAIRAAERRLKEASIERDTLE 296
|
..
gi 31982223 1779 AR 1780
Cdd:pfam19220 297 RR 298
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1144-1188 |
6.74e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 6.74e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 1144 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1188
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1603-1783 |
6.87e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1603 QKAETVQAALEEAQRAQGAAQGAiwgaVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAA 1682
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1683 STAEEtagsaQSRAREAEKQLRE--QVGDQYQTVRA-LAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGT 1759
Cdd:COG4717 140 ELAEL-----PERLEELEERLEElrELEEELEELEAeLAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180
....*....|....*....|....
gi 31982223 1760 YEENERALEGKAAQLDGLEARMRS 1783
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEA 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1454-1793 |
7.36e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.00 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1454 LGRARhtqAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELreliQNVKDFLSQEGADPDS 1533
Cdd:COG4372 8 VGKAR---LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL----EQLEEELEQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1534 IEmvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKaetVQAALE 1613
Cdd:COG4372 78 LE---------------EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ---LEAQIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1614 EAQRAQGAAQGAIwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERA--RQLDALLEALKLKRAGNSLAASTAEETAGS 1691
Cdd:COG4372 140 ELQSEIAEREEEL-------KELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1692 AQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKA 1771
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
330 340
....*....|....*....|..
gi 31982223 1772 AQLDGLEARMRSVLQAINLQVQ 1793
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALE 314
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1476-1782 |
1.03e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.82 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1476 SRVSETRRQAEE-AQQRAQAALDKanasrgqveqanQELRELIQNVKDFLSQEGA---DPDSIEMVAT-----RVLDISI 1546
Cdd:COG3096 785 KRLEELRAERDElAEQYAKASFDV------------QKLQRLHQAFSQFVGGHLAvafAPDPEAELAAlrqrrSELEREL 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1547 PASPEQIQRLASEIAERVRSLADVDTILAHTMgdvrraeqLLQDAHRArsraegerQKAETVQAALEEAQRAQG--AAQG 1624
Cdd:COG3096 853 AQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN--------LLADETLA--------DRLEELREELDAAQEAQAfiQQHG 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1625 AiWGAVVDTQntEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALK--LKR--------AGNSLAASTAE-------- 1686
Cdd:COG3096 917 K-ALAQLEPL--VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevVQRrphfsyedAVGLLGENSDLneklrarl 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1687 ETAGSAQSRAREAEKQLREQVgDQY---------------QTVRALAERKAE-GVLAAQARAEQLRDEARDLLQAAQDKL 1750
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQY-SQYnqvlaslkssrdakqQTLQELEQELEElGVQADAEAEERARIRRDELHEELSQNR 1072
|
330 340 350
....*....|....*....|....*....|..
gi 31982223 1751 QRLQELEGTYEENEralegkaAQLDGLEARMR 1782
Cdd:COG3096 1073 SRRSQLEKQLTRCE-------AEMDSLQKRLR 1097
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1575-1790 |
1.16e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1575 AHTMGD---VRRAEQLLQDAHRARSRAEGERQKAE----TVQAALEEAQRAQGA--AQGAIWGAV-------VDTQNTEQ 1638
Cdd:COG4913 589 RHEKDDrrrIRSRYVLGFDNRAKLAALEAELAELEeelaEAEERLEALEAELDAlqERREALQRLaeyswdeIDVASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1639 TLQRVQERMAGAEKS---LNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVR 1715
Cdd:COG4913 669 EIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1716 ALAERKAEGvLAAQARAEQLRDEARDLLQAAQDKLQRL-QELEGTYEENERALEGKAAQLD-GLEA-----RMRSVLQAI 1788
Cdd:COG4913 749 ALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAeEELERAMRAFNREWPAETADLDaDLESlpeylALLDRLEED 827
|
..
gi 31982223 1789 NL 1790
Cdd:COG4913 828 GL 829
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1444-1788 |
1.21e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.69 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1444 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1522
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1523 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1589
Cdd:NF041483 984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1590 DAHRA--RSRAEGERQKAETVQAALEEAQRAQGAAqgaiwgAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDAL 1667
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERIVAEA------TVEGNSLVEKARTDADELLVGARRDATAIRERAEELRDR 1129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1668 LE--------------ALKLKRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AAQ 1729
Cdd:NF041483 1130 ITgeieelherarresAEQMKSAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAEQ 1205
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1730 ARAEQLRdeardllQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEA---RMRSVLQAI 1788
Cdd:NF041483 1206 KKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1580-1777 |
1.21e-09 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 60.78 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1580 DVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQR---AQGAAQGAIWGAVVDTQNTEQ----------TLQRVQER 1646
Cdd:pfam12795 21 DLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQelaALQAKAEAAPKEILASLSLEEleqrllqtsaQLQELQNQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1647 MAGAEKSLNSAGERARQLDALLEALK--LKRAGNSLAASTAEETA-GSAQSRAREAEKQLREQVGDQYQ------TVR-A 1716
Cdd:pfam12795 101 LAQLNSQLIELQTRPERAQQQLSEARqrLQQIRNRLNGPAPPGEPlSEAQRWALQAELAALKAQIDMLEqellsnNNRqD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1717 LAERKAEgvlAAQARAEQLrDEARDLLQAAQDKlQRLQELEGTYEENERALEGKAAQLDGL 1777
Cdd:pfam12795 181 LLKARRD---LLTLRIQRL-EQQLQALQELLNE-KRLQEAEQAVAQTEQLAEEAAGDHPLV 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1475-1783 |
1.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQelreliqnvKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQ 1554
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK---------AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1555 RLASEIAERVRSLADVDTILAHTMGDVRRAEQlLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGaiwgavvdtq 1634
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA---------- 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1635 nteQTLQRVQERMAGAEKSLNSAgERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTV 1714
Cdd:PTZ00121 1447 ---DEAKKKAEEAKKAEEAKKKA-EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982223 1715 RALAERKAEgvlaAQARAEQLRdEARDLLQAaqDKLQRLQELEGTyEENERALEGKAAQLDGLEARMRS 1783
Cdd:PTZ00121 1523 KADEAKKAE----EAKKADEAK-KAEEKKKA--DELKKAEELKKA-EEKKKAEEAKKAEEDKNMALRKA 1583
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1446-1797 |
1.34e-09 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 61.98 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAELQR----ALVEGGGIlsrvsetRRQAEEAQQRAQAAldkanasrgqVEQANQELRELIQNV- 1520
Cdd:COG1538 17 RAARARVEAARAQLRQARAGLlpsqELDLGGKR-------RARIEAAKAQAEAA----------EADLRAARLDLAAEVa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1521 KDFLSQEGADpdsiemvatRVLDISipaspEQIQRLASEIAERVRSLADVDTIlahTMGDVRRAEQLLQDAHRARSRAEG 1600
Cdd:COG1538 80 QAYFDLLAAQ---------EQLALA-----EENLALAEELLELARARYEAGLA---SRLDVLQAEAQLAQARAQLAQAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1601 ERQKAETV-QAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQER---MAGAEkslnsageraRQLDALLEALKLKRA 1676
Cdd:COG1538 143 QLAQARNAlALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERrpdLRAAE----------AQLEAAEAEIGVARA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1677 GN----SLAAS---TAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEA----RDLLQA 1745
Cdd:COG1538 213 AFlpslSLSASygySSSDDLFSGGSDTWSVGLSLSLPLFDGGRNRARVRAAKAQ-LEQAEAQYEQTVLQAlqevEDALAA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982223 1746 AQDKLQRLQELEGTYEENERALE--------GKAAQLDGLEARmRSVLQA----INLQVQIYNT 1797
Cdd:COG1538 292 LRAAREQLEALEEALEAAEEALElararyraGLASLLDVLDAQ-RELLQAqlnlIQARYDYLLA 354
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1038-1094 |
1.35e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.35e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1038 RCTCNLLGTDPRRCpstdlchcDPSTGQCPCLPHVQGLNCDHCAPNFWNFTS-GRGCQ 1094
Cdd:cd00055 1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1446-1747 |
1.40e-09 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 62.73 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLAlGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDfls 1525
Cdd:COG0840 273 AASAEELA-AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 qegadpdsiemVATRVLDISipASPEQIqrlaSEIaervrsladVDTIlahtmGDVrrAEQ--LLQ-----DAHRArsra 1598
Cdd:COG0840 349 -----------TAETIEELG--ESSQEI----GEI---------VDVI-----DDI--AEQtnLLAlnaaiEAARA---- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1599 eGERQK-----AETVQAaLeeAQRAQGAaqgaiwgavvdTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEalkl 1673
Cdd:COG0840 392 -GEAGRgfavvADEVRK-L--AERSAEA-----------TKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVE---- 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1674 kRAGNSLA--ASTAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQ 1747
Cdd:COG0840 453 -EAGEALEeiVEAVEEVSDLIQEIAAASEEQSAgtEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
473-527 |
1.47e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 1.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 473 CQCNSRGTVpgSSPCDSSSGTCFCKRLVTGHGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1096-1141 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 1.79e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 1096 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDPGLQC 1141
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1462-1777 |
2.03e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.89 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1462 AELQRALVEgggILSRVSETRRQ---AEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGAD-------- 1530
Cdd:pfam01576 218 TDLQEQIAE---LQAQIAELRAQlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqr 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1531 ---PDSIEMVATRVLDI--SIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRR---------AEQLLQdAHRARS 1596
Cdd:pfam01576 295 rdlGEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelTEQLEQ-AKRNKA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1597 RAEGERQKAETVQAAL-EEAQRAQGAAQgaiwgavvDTQN----TEQTLQRVQERMAGAEKSLNSAGERARQLDALLEAL 1671
Cdd:pfam01576 374 NLEKAKQALESENAELqAELRTLQQAKQ--------DSEHkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1672 ---------KLKRAGNSLAASTA----------EET----AGSAQSRAREAEKQ-LREQ----------VGDQYQTVRA- 1716
Cdd:pfam01576 446 ssllneaegKNIKLSKDVSSLESqlqdtqellqEETrqklNLSTRLRQLEDERNsLQEQleeeeeakrnVERQLSTLQAq 525
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31982223 1717 LAE--RKAEGVLAAqarAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGL 1777
Cdd:pfam01576 526 LSDmkKKLEEDAGT---LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-523 |
2.36e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 2.36e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 31982223 472 RCQCNSRGTVPGSspCDSSSGTCFCKRLVTGHGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1095-1142 |
2.68e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.28 E-value: 2.68e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1095 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDP--GLQCR 1142
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
412-471 |
3.10e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.28 E-value: 3.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASDPRGCQ 471
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1551-1759 |
3.25e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIAERVRSLADVDTILA------HTMGDVRRAEQLLQD----------AHRARSRAEGERQKAE-------T 1607
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEaleaelDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDassddlaA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1608 VQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQ-----LDALLEALKLKRAGNSLAA 1682
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1683 STAEETAGsAQSRAREAEKQLREQVGD---QYQTVRALAERKAEGVLAAQARAEQLRDEarDLLQAAQDKLQRLQELEGT 1759
Cdd:COG4913 770 NLEERIDA-LRARLNRAEEELERAMRAfnrEWPAETADLDADLESLPEYLALLDRLEED--GLPEYEERFKELLNENSIE 846
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1486-1792 |
3.68e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1486 EEAQQRAQAALDKANAS-RGQVEQANQELRELIQNVKDFLSQEGadpdsiemvatrvldisIPASPEQIQRLASEIAErv 1564
Cdd:COG3206 163 EQNLELRREEARKALEFlEEQLPELRKELEEAEAALEEFRQKNG-----------------LVDLSEEAKLLLQQLSE-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1565 rsladvdtilahtmgdvrraeqlLQDahrARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVdTQNTEQTLQRVQ 1644
Cdd:COG3206 224 -----------------------LES---QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1645 ERMAGAEKSLNSAGERARQLDALLEALklkragnslaastaeetagsaqsrareaEKQLREQVGdqyqtvRALAERKAEg 1724
Cdd:COG3206 277 AELAELSARYTPNHPDVIALRAQIAAL----------------------------RAQLQQEAQ------RILASLEAE- 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1725 VLAAQARAEQLRDEardlLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQV 1792
Cdd:COG3206 322 LEALQAREASLQAQ----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1450-1741 |
3.69e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1450 ADLALGRARhtQAELQRALVEGGGILSRVSETRRQAEEAQQ-----RAQAAL-------DKANASRGQVEQANQELRELI 1517
Cdd:COG3096 836 AELAALRQR--RSELERELAQHRAQEQQLRQQLDQLKEQLQllnklLPQANLladetlaDRLEELREELDAAQEAQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1518 QN------VKDFLSQEGADPDSIEMVATRVLDISipASPEQIQRLA---SEIAERVRSLA--DVDTILAHTMGDVRRAEQ 1586
Cdd:COG3096 914 QHgkalaqLEPLVAVLQSDPEQFEQLQADYLQAK--EQQRRLKQQIfalSEVVQRRPHFSyeDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1587 LLQDAHRARSRAegeRQKAETVQAALEEAQRAQGAAQGAiwgavvdTQNTEQTLQRVQERM--------AGAEkslNSAG 1658
Cdd:COG3096 992 RLEQAEEARREA---REQLRQAQAQYSQYNQVLASLKSS-------RDAKQQTLQELEQELeelgvqadAEAE---ERAR 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1659 ERARQLDALLEALKLKRagnslaaSTAEETAGSAQSRAREAEKQLREqVGDQYQTVRalaerkaEGVLAAQARAEQLRDE 1738
Cdd:COG3096 1059 IRRDELHEELSQNRSRR-------SQLEKQLTRCEAEMDSLQKRLRK-AERDYKQER-------EQVVQAKAGWCAVLRL 1123
|
...
gi 31982223 1739 ARD 1741
Cdd:COG3096 1124 ARD 1126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1461-1787 |
4.08e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1461 QAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQAN-------QELR------------------E 1515
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparlLALRdalaealgldeaelpfvgE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1516 LIQNVKDFLSQEGAdpdsIEMV-ATRVLDISIPasPEQIQRlASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDA--- 1591
Cdd:COG4913 466 LIEVRPEEERWRGA----IERVlGGFALTLLVP--PEHYAA-ALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSlag 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1592 ------HRARSRAEGE------RQKAETVQAaLEEAQRA--------QGAAQGAIWGAVVDTQ-------NTEQtLQRVQ 1644
Cdd:COG4913 539 kldfkpHPFRAWLEAElgrrfdYVCVDSPEE-LRRHPRAitragqvkGNGTRHEKDDRRRIRSryvlgfdNRAK-LAALE 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1645 ERMAGAEKSLNSAGERARQLDALLEAL-KLKRAGNSLAASTAEET-AGSAQSRAREAEKQLREqvgdqyqtvraLaeRKA 1722
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALqERREALQRLAEYSWDEIdVASAEREIAELEAELER-----------L--DAS 683
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1723 EGVLAA-QARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQA 1787
Cdd:COG4913 684 SDDLAAlEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1548-1789 |
4.65e-09 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 60.82 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1548 ASPEQIQRLASEIAERVRSLADVDTILAhtMGDVRRAEQllqdaHRARSRAEGERQKAETVqaalEEAQRAQGAAqgaiw 1627
Cdd:COG3064 19 EQAEAEKRAAAEAEQKAKEEAEEERLAE--LEAKRQAEE-----EAREAKAEAEQRAAELA----AEAAKKLAEA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1628 gavvdtqntEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNslAASTAEETA-GSAQSRAREAEKQ-LRE 1705
Cdd:COG3064 83 ---------EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AKRKAEEEAkRKAEEERKAAEAEaAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1706 QVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVL 1785
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
....
gi 31982223 1786 QAIN 1789
Cdd:COG3064 232 AALA 235
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
831-873 |
5.86e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.51 E-value: 5.86e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 31982223 831 ACQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFP 873
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1582-1793 |
6.91e-09 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 60.44 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1582 RRAEQLLQdahRARSRAEGERQ-KAETVQAALEEAQRAQGAAQGAiwgavvdTQNTEQtlQRVQERMAGAEKSLNSAGER 1660
Cdd:COG3064 8 KAAEAAAQ---ERLEQAEAEKRaAAEAEQKAKEEAEEERLAELEA-------KRQAEE--EAREAKAEAEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1661 ARQLDallealKLKRAGNSLAASTAEETAgsaqSRAREAEKQLREQVGDQYQTVRALAE--RKAEGvlAAQARAEQLRDE 1738
Cdd:COG3064 76 AKKLA------EAEKAAAEAEKKAAAEKA----KAAKEAEAAAAAEKAAAAAEKEKAEEakRKAEE--EAKRKAEEERKA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1739 ARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQ 1793
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1453-1787 |
7.91e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.96 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1453 ALGRARHTQA-ELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQV--------------EQANQELRELI 1517
Cdd:pfam01576 629 AEAREKETRAlSLARALEE-------ALEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskralEQQVEEMKTQL 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1518 QNVKDFLsQEGADpdsiemvATRVLDISIPASPEQIQRLAS---EIAE-RVRSLADvdtilahtmgDVRRAEQLLQDAHR 1593
Cdd:pfam01576 702 EELEDEL-QATED-------AKLRLEVNMQALKAQFERDLQardEQGEeKRRQLVK----------QVRELEAELEDERK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1594 ARSRAEGERQKAET----VQAALEEAQRAQGAAQGAIWGAvvdtQNTEQTLQR-VQERMAGAEKSLNSAGERARQLDAlL 1668
Cdd:pfam01576 764 QRAQAVAAKKKLELdlkeLEAQIDAANKGREEAVKQLKKL----QAQMKDLQReLEEARASRDEILAQSKESEKKLKN-L 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1669 EAlKLKRAGNSLAAST-------------AEETAGSAQSRAREAEK---------QLREQVGDQYQTVRALAERKAEGV- 1725
Cdd:pfam01576 839 EA-ELLQLQEDLAASErarrqaqqerdelADEIASGASGKSALQDEkrrleariaQLEEELEEEQSNTELLNDRLRKSTl 917
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1726 --------LAAQARAEQLRDEARDLLQAAQDKLQ-RLQELEGT----YEENERALEGKAAQL-DGLEARMRSVLQA 1787
Cdd:pfam01576 918 qveqltteLAAERSTSQKSESARQQLERQNKELKaKLQEMEGTvkskFKSSIAALEAKIAQLeEQLEQESRERQAA 993
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1475-1779 |
9.15e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisiPASPEQIQ 1554
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEE-----------AKKADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1555 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLLQDAHRARsRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVD 1632
Cdd:PTZ00121 1451 KKAEEAkkAEEAKKKAE----------EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1633 TQNTEQTLQRVQERMAGAEksLNSAgERARQLDALLEALKLKRAGNSLAASTA---EETAGSAQSRA---REAEKQLREQ 1706
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADE--AKKA-EEKKKADELKKAEELKKAEEKKKAEEAkkaEEDKNMALRKAeeaKKAEEARIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1707 VGDQYQTVRALAERKAEGVLAAQARAEQLRDE------ARDLLQAAQDKLQRLQELEGTYEENE--RALEGKAAQLDGLE 1778
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeekkkVEQLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKK 1676
|
.
gi 31982223 1779 A 1779
Cdd:PTZ00121 1677 A 1677
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
832-873 |
9.28e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 9.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 31982223 832 CQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFP 873
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1039-1093 |
1.01e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1039 CTCNLLGTDPRrcpstdlcHCDPSTGQCPCLPHVQGLNCDHCAPNFWNFtSGRGC 1093
Cdd:smart00180 1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
525-564 |
1.09e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.09e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 31982223 525 CDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFR 564
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1450-1791 |
1.11e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1450 ADLALGRARHTQAELQRALVEG--GGILSRVSETRRQAEEAQQR---AQAALDKANASRGQVEQANqelrelIQNVKDFL 1524
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEGqlQELQARLSESERQRAELAEKlskLQSELESVSSLLNEAEGKN------IKLSKDVS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1525 SQEGADPDSIEMVA--TRvldisipaspeqiQRLAseIAERVRSLADVDTILAhtmgdvrraEQLLQDAhraRSRAEGER 1602
Cdd:pfam01576 465 SLESQLQDTQELLQeeTR-------------QKLN--LSTRLRQLEDERNSLQ---------EQLEEEE---EAKRNVER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1603 QkAETVQAALEEAQRAQGAAQGAIWGAVVD----TQNTEQTLQRVQERMAGAEKsLNSAGERARQ-LDALLEALKLKRag 1677
Cdd:pfam01576 518 Q-LSTLQAQLSDMKKKLEEDAGTLEALEEGkkrlQRELEALTQQLEEKAAAYDK-LEKTKNRLQQeLDDLLVDLDHQR-- 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1678 nSLAAST-----------AEETAGSAQsRARE---AEKQLREQVGDQYQTVRALAErkaegvlAAQARAE------QLRD 1737
Cdd:pfam01576 594 -QLVSNLekkqkkfdqmlAEEKAISAR-YAEErdrAEAEAREKETRALSLARALEE-------ALEAKEElertnkQLRA 664
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982223 1738 EARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLE--------ARMR-SV-LQAINLQ 1791
Cdd:pfam01576 665 EMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEdelqatedAKLRlEVnMQALKAQ 728
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1462-1772 |
1.12e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 60.04 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1462 AELQrALVEGggILSRVSETRRQAEEAQQRAQAALDKANAS----RGQVEQANQE---LRELIQNVKDFLSQEGADPDSI 1534
Cdd:pfam05701 264 AELA-AYMES--KLKEEADGEGNEKKTSTSIQAALASAKKEleevKANIEKAKDEvncLRVAAASLRSELEKEKAELASL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1535 ---EMVATrvldISIPASPEQIQRLASEIAervrsladvdtiLAHTMGDVRRAE-----QLLQDAHRARSRAEGERQKA- 1605
Cdd:pfam05701 341 rqrEGMAS----IAVSSLEAELNRTKSEIA------------LVQAKEKEAREKmvelpKQLQQAAQEAEEAKSLAQAAr 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1606 ETVQAALEEAQRAQGAAQgaiwgavvdtqNTEQTLQRVQERMAGAEKSLNSAGERARqldALLEALKLKRAGNSLAAS-- 1683
Cdd:pfam05701 405 EELRKAKEEAEQAKAAAS-----------TVESRLEAVLKEIEAAKASEKLALAAIK---ALQESESSAESTNQEDSPrg 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1684 ---TAEETAgSAQSRAREAEKQLREQVgdqyqtVRALAERKAegvlaaqARAEQLRDEARdLLQAAQDKLQRLQELEGTY 1760
Cdd:pfam05701 471 vtlSLEEYY-ELSKRAHEAEELANKRV------AEAVSQIEE-------AKESELRSLEK-LEEVNREMEERKEALKIAL 535
|
330
....*....|..
gi 31982223 1761 EENERALEGKAA 1772
Cdd:pfam05701 536 EKAEKAKEGKLA 547
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1445-1794 |
1.37e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 59.54 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1445 GAAATADLALGRARHTQAELQRALVegggILSRVSETRRQAEEAQ--QRA------QAALDKANASRGQVEQANQELREL 1516
Cdd:COG5278 23 VLGVLSYLSLNRLREASEWVEHTYE----VLRALEELLSALLDAEtgQRGylltgdESFLEPYEEARAEIDELLAELRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1517 IQNvkdflsqegadpdsiemvatrvldisipaSPEQIQRLAS--EIAERVRSLADvDTILAHTMGDVRRAEQLLQ----- 1589
Cdd:COG5278 99 TAD-----------------------------NPEQQARLDEleALIDQWLAELE-QVIALRRAGGLEAALALVRsgegk 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1590 ---DAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDA 1666
Cdd:COG5278 149 almDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1667 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAA 1746
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 31982223 1747 QDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQI 1794
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1582-1790 |
1.81e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1582 RRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGER- 1660
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1661 ARQLDALLEALKLKRAGNSLAASTAEETAGSAQ-----SRAREAE-KQLREQVGDQYQTVRALAERKAE------GVLAA 1728
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQaEELRADLAELAALRAELEAERAEleallaELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1729 QARAEQLRDEARDLLQAAQDKL----QRLQELegtyEENERALEGKAAQLDGLEARMRSVLQAINL 1790
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELaelaAELAEL----QQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1452-1779 |
2.09e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1452 LALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEQANQELRELIQNVKDFLSQEGADP 1531
Cdd:pfam07888 24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD-------REQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1532 DSIEMVATRVLDISIPASPEQIQRLASEIA--ERVRSLADVDTILAHTMGD----VRRAEQLLQDAHRARSRAEGERQKA 1605
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAheARIRELEEDIKTLTQRVLEreteLERMKERAKKAGAQRKEEEAERKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1606 ET-VQAALEEAQRAQGAAQGAI-WGAVVDTQnteqtLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRagNSLAAS 1683
Cdd:pfam07888 177 QAkLQQTEEELRSLSKEFQELRnSLAQRDTQ-----VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ--ERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1684 --TAE------ETAGSAQSRAREAEKQLREQVGDqyqtvraLAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQE 1755
Cdd:pfam07888 250 erKVEglgeelSSMAAQRDRTQAELHQARLQAAQ-------LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEK 322
|
330 340
....*....|....*....|....
gi 31982223 1756 LEGTYEENERALEGKAAQLDGLEA 1779
Cdd:pfam07888 323 LSAELQRLEERLQEERMEREKLEV 346
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
987-1029 |
2.85e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 2.85e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 31982223 987 CECSGNIDPmdPDACDPHTGQCLrCLHNTEGPHCGYCKPGFHG 1029
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1447-1747 |
2.85e-08 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 58.85 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1447 AATADLALGRARHTQAELQRAL------VEGGGIlsrvsetrRQAEEAQQRAQAALDKA---NASRGQVEQANQELRELI 1517
Cdd:pfam13779 451 SALARLELARSDEALDEVADLLwelalrIEDGDL--------SDAERRLRAAQERLSEAlerGASDEEIAKLMQELREAL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1518 QnvkDFLSQ-------EGADPDSIEMVATRVLdisipaSPEQIQRLASEIAERVRSladvdtilahtmGDVRRAEQLLQD 1590
Cdd:pfam13779 523 D---DYMQAlaeqaqqNPQDLQQPDDPNAQEM------TQQDLQRMLDRIEELARS------------GRRAEAQQMLSQ 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1591 ------------AHRARSRAEGERQKA-----ETV---QAALEEAQR----AQGAAQGAIWGAVVDTQNTEQTLQRVQER 1646
Cdd:pfam13779 582 lqqmlenlqagqPQQQQQQGQSEMQQAmdelgDLLreqQQLLDETFRqlqqQGGQQQGQPGQQGQQGQGQQPGQGGQQPG 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1647 MAGAEKSL-NSAGERARQLDALLEAL-KLKRAGNSLAASTAEETAGSAQSRAREAEKqlreqvgdqyqtvrALAERKAEG 1724
Cdd:pfam13779 662 AQMPPQGGaEALGDLAERQQALRRRLeELQDELKELGGKEPGQALGDAGRAMRDAEE--------------ALGQGDLAG 727
|
330 340
....*....|....*....|....
gi 31982223 1725 VLAAQARA-EQLRDEARDLLQAAQ 1747
Cdd:pfam13779 728 AVDAQGRAlEALRKGAQQLAEAMQ 751
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1484-1756 |
2.90e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 58.91 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1484 QAE--EAQQRAQAALDKANASRGQVEQANQ---ELRELIQNVKDFLSQEGADPDSIEmvatrvLDISIPASPEQIQRLAS 1558
Cdd:PRK10929 43 QAEivEALQSALNWLEERKGSLERAKQYQQvidNFPKLSAELRQQLNNERDEPRSVP------PNMSTDALEQEILQVSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1559 EIAE----------RVRSLADVDTILAhtmgdvrraeQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWG 1628
Cdd:PRK10929 117 QLLEksrqaqqeqdRAREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1629 AVVD-------TQNTEQTLQRVQERMagAEKslnsageRARQLDALLEALKlkragNSLAASTAEETagsaqSRAREAEK 1701
Cdd:PRK10929 187 ALVDelelaqlSANNRQELARLRSEL--AKK-------RSQQLDAYLQALR-----NQLNSQRQREA-----ERALESTE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31982223 1702 QLREQVGD-------QYQTVRALAErkaegVLAAQA-RAEQLRDEARdllQAAQDKLQRLQEL 1756
Cdd:PRK10929 248 LLAEQSGDlpksivaQFKINRELSQ-----ALNQQAqRMDLIASQQR---QAASQTLQVRQAL 302
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1444-1762 |
3.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1444 SGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASrgqveqanqelrELIQNVKDF 1523
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP------------ECGQPVEGS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1524 LSQEGADPD--SIEMVATRVLDISipaspEQIQRLASEIaERVRSLADVDTILAHTMGDVRRAEQLLQDAH----RARSR 1597
Cdd:PRK02224 465 PHVETIEEDreRVEELEAELEDLE-----EEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRetieEKRER 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1598 AEGERQKAETVQAALEE----AQRAQGAAQGAIwgAVVDTQNTEQT--------LQRVQERMAGAEKSLNSAGERARQLD 1665
Cdd:PRK02224 539 AEELRERAAELEAEAEEkreaAAEAEEEAEEAR--EEVAELNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKRE 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1666 ALLEA-------LKLKRAGNS-LAASTAEETAGSAQSRAREAEKQLrEQVGDQyqtVRALAERKAE------GVLAAQAR 1731
Cdd:PRK02224 617 ALAELnderrerLAEKRERKReLEAEFDEARIEEAREDKERAEEYL-EQVEEK---LDELREERDDlqaeigAVENELEE 692
|
330 340 350
....*....|....*....|....*....|....*
gi 31982223 1732 AEQLRDEaRDLLQAAQDKLQRL----QELEGTYEE 1762
Cdd:PRK02224 693 LEELRER-REALENRVEALEALydeaEELESMYGD 726
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1453-1682 |
3.48e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.99 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1453 ALGRARHTQAEL--QRALVEgggilSRVSETRRQAEEAQQRAQAALDKANasrgqveqanqelreliqnvkdflsqegad 1530
Cdd:COG1842 38 DLVEARQALAQViaNQKRLE-----RQLEELEAEAEKWEEKARLALEKGR------------------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1531 pdsiEMVATRVLdisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAhrarsraegeRQKAETVqA 1610
Cdd:COG1842 83 ----EDLAREAL--------ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEL----------KAKKDTL-K 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1611 ALEEAQRAQGAAQGAIWGavVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQ--LDALLEALKLKRAGNS-LAA 1682
Cdd:COG1842 140 ARAKAAKAQEKVNEALSG--IDSDDATSALERMEEKIEEMEARAEAAAELAAGdsLDDELAELEADSEVEDeLAA 212
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1450-1681 |
3.65e-08 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 55.84 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1450 ADLALGRARHTQAEL---QRALVEgggilsRVSETRRQAEEAQQRAQAALDKanasrgqveqANQEL-RELIQnvkdfls 1525
Cdd:pfam04012 34 MQSELVKARQALAQTiarQKQLER------RLEQQTEQAKKLEEKAQAALTK----------GNEELaREALA------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 qegadpdsiemvatrvldisipaspeQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAhrarsraegeRQKA 1605
Cdd:pfam04012 91 --------------------------EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL----------KAKK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1606 ETVQAAlEEAQRAQGAAQGAIWGAvvDTQNTEQTLQRVQERMAGAEKSLNSAGERA--RQLDALLEALKLKRAGNSLA 1681
Cdd:pfam04012 135 NLLKAR-LKAAKAQEAVQTSLGSL--STSSATDSFERIEEKIEEREARADAAAELAsaVDLDAKLEQAGIQMEVSEDV 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1198-1753 |
3.72e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1198 WDRVVQDLAARTRRLEQWAQELQQtgvLGAFESSFLNMQGKLGMVQAiMSARNASAASTAKLVEATEGLRHEIGKTTERL 1277
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE---LEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1278 TQLEAELTAVQDenfnanhalsgLERDGLALNLTLRQLDQHLEILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAVps 1357
Cdd:COG4717 149 EELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1358 pvsnsADTRRRTEVLMgAQKENFNRQHLAnQQALGRLSAHAHTLSLTGInelvcgapgdapcatspcggagcrdedgqpR 1437
Cdd:COG4717 216 -----EEAQEELEELE-EELEQLENELEA-AALEERLKEARLLLLIAAA------------------------------L 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1438 CGGLGCSGAAATADLALGRArhtqaelqrALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasrgqveqANQELREli 1517
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGV---------LFLVLGLLALLFLLLAREKASLGKEAEELQALP---------ALEELEE-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1518 QNVKDFLSQEGADPD-SIEMVATRVLDIsipaspEQIQRLASEIAERVRSL------ADVDTILAHtmGDVRRAEQLLQD 1590
Cdd:COG4717 319 EELEELLAALGLPPDlSPEELLELLDRI------EELQELLREAEELEEELqleeleQEIAALLAE--AGVEDEEELRAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1591 AHRARSRAEgERQKAETVQAALEEAQRAQGAAQgaiwgAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEA 1670
Cdd:COG4717 391 LEQAEEYQE-LKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1671 LklkragnslaastaeETAGSAqSRAREAEKQLREQvgdqyqtVRALAERKAEGVLAAQArAEQLRDEARD-----LLQA 1745
Cdd:COG4717 465 L---------------EEDGEL-AELLQELEELKAE-------LRELAEEWAALKLALEL-LEEAREEYREerlppVLER 520
|
....*...
gi 31982223 1746 AQDKLQRL 1753
Cdd:COG4717 521 ASEYFSRL 528
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1197-1793 |
4.08e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.44 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1197 DWDRVVQDLAARTRRLeqwAQELQQTGVLGAFESSFLNMQGKLGMVQAiMSARNASAASTAKLVEATEGLRHEIgktTER 1276
Cdd:TIGR00618 308 QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTL---TQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1277 LTQLEAELTAVQDENFNANHALSGLERD-GLALNLTLRQ--LDQHLEILKHSNFLgaydSIRHAHSQSTEAERRANASTF 1353
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFrdLQGQLAHAKKQQEL----QQRYAELCAAAITCTAQCEKL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1354 AVPSPVSNSADTRRRTEVLmgAQKENFNRQHLANQQAlgrlsaHAHTLSLTGINE-LVCGA---PGDAPCATSPCGGAGC 1429
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAV------VLARLLELQEEPcPLCGScihPNPARQDIDNPGPLTR 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1430 RDEDGQPRCGGLGCSGAaatadlalgrarHTQAELQralveggGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQa 1509
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEE------------DVYHQLT-------SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN- 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1510 nqeLRELIQNVKDFLSQEGADPDSIEMVATRVLdisIPASPEQ-IQRLASEIAERVRSLADVDTILAhtmgdvRRAEQLL 1588
Cdd:TIGR00618 589 ---LQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQdLQDVRLHLQQCSQELALKLTALH------ALQLTLT 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1589 QD--AHRARSRAEGERQKAETVQAALEEAQRAQgaAQGAIWgavvdtqntEQTLQRVQERMAGAEKSLNSAGERARQLDA 1666
Cdd:TIGR00618 657 QErvREHALSIRVLPKELLASRQLALQKMQSEK--EQLTYW---------KEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1667 LLEALKLKRAGNSlaaSTAEETAGSAQsraREAEKQLREQVGDQyqtvralaERKAEGVLAAQARaeqlrdeardllqaa 1746
Cdd:TIGR00618 726 ASSSLGSDLAARE---DALNQSLKELM---HQARTVLKARTEAH--------FNNNEEVTAALQT--------------- 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1747 qdkLQRLQELEGTYEENERALEGKAAQLDGLEARMR----SVLQAINLQVQ 1793
Cdd:TIGR00618 777 ---GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCE 824
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1731-1798 |
4.26e-08 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 51.59 E-value: 4.26e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1731 RAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTC 1798
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1629-1788 |
1.08e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1629 AVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVG 1708
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1709 DQYQT-------------------------VRALAERKAEgVLAAQARAEQLRDEARDLLQAAQDKLQRLQ-ELEGTYEE 1762
Cdd:COG3883 94 ALYRSggsvsyldvllgsesfsdfldrlsaLSKIADADAD-LLEELKADKAELEAKKAELEAKLAELEALKaELEAAKAE 172
|
170 180
....*....|....*....|....*.
gi 31982223 1763 NERALEGKAAQLDGLEARMRSVLQAI 1788
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
413-466 |
1.17e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 1.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 31982223 413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASD 466
Cdd:smart00180 1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1490-1790 |
1.23e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 56.62 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1490 QRAQAALDKANASRGQVEqANQELRELiQNVKDFLSQEGADPDSIEMVATRVLDIS---------IPASPEQIQRLAS-- 1558
Cdd:COG0497 48 GRADASLVRHGADKAEVE-AVFDLSDD-PPLAAWLEENGLDLDDGELILRREISADgrsrafingRPVTLSQLRELGEll 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1559 -EI-----------AERVRSL----ADVDTILAhtmgDVRRAEQLLQDAHRARSRAEGE----RQKAETVQAALEEAQRA 1618
Cdd:COG0497 126 vDIhgqhehqslldPDAQRELldafAGLEELLE----EYREAYRAWRALKKELEELRADeaerARELDLLRFQLEELEAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1619 QGAAqgaiwgavvdtqNTEQTLQRVQERMAGAEKsLNSAGERARQ---------LDALLEAL----KLKRAGNSLAAstA 1685
Cdd:COG0497 202 ALQP------------GEEEELEEERRRLSNAEK-LREALQEALEalsggeggaLDLLGQALraleRLAEYDPSLAE--L 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1686 EETAGSAQSRAREAEKQLR-------------EQVGDQYQTVRALAeRK----AEGVLAaqaraeqLRDEARDLLQAAQD 1748
Cdd:COG0497 267 AERLESALIELEEAASELRryldslefdperlEEVEERLALLRRLA-RKygvtVEELLA-------YAEELRAELAELEN 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1749 KLQRLQELEGTYEENERALEGKAAQL--------DGLEARMRSVLQAINL 1790
Cdd:COG0497 339 SDERLEELEAELAEAEAELLEAAEKLsaarkkaaKKLEKAVTAELADLGM 388
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1787 |
1.32e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 56.76 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAEL---------QRALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasRGQVEQANQELREL 1516
Cdd:NF041483 277 ARAEAEKVVAEAKEAAAKQlasaesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADA---RAEAEKLVAEAAEK 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1517 IQNV--KDFLSQEGADPDSIEMVATRVLD---ISIPASPEQIQRL--------------ASEIAERVRSLADVDT--ILA 1575
Cdd:NF041483 354 ARTVaaEDTAAQLAKAARTAEEVLTKASEdakATTRAAAEEAERIrreaeaeadrlrgeAADQAEQLKGAAKDDTkeYRA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1576 HTM---GDVRR----AEQLlqdahRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTlqrvqermA 1648
Cdd:NF041483 434 KTVelqEEARRlrgeAEQL-----RAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRST--------A 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1649 GAEkslnsaGERARQlDALLEALKLKRagnslaasTAEETAgsaqSRAREAEKQLREQVGDQYQTVRALAERKAE----- 1723
Cdd:NF041483 501 TAE------SERVRT-EAIERATTLRR--------QAEETL----ERTRAEAERLRAEAEEQAEEVRAAAERAARelree 561
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1724 ---GVLAAQARA----EQLRDEARDLLQAAQdklqrlQELEGTYEENERALEGKAAQLDGLEA----RMRSvLQA 1787
Cdd:NF041483 562 terAIAARQAEAaeelTRLHTEAEERLTAAE------EALADARAEAERIRREAAEETERLRTeaaeRIRT-LQA 629
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1486-1788 |
1.37e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1486 EEAQQRAQAALDKANASRGQVEQANQELRELIQNVkDFLSQEGADPDSIEMVATRVLDI-------SIPASPEQIQRLAS 1558
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYegyellkEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1559 EIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHrARSRAEGE------RQKAETVQAALEEAQRAQGAAqgaiwgavvd 1632
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEeeqlrvKEKIGELEAEIASLERSIAEK---------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1633 tqntEQTLQRVQERMAGAEKSLNSAGERARQLDallealklkragnslaastaeetagsaqsRAREAEKQLREQVGDQY- 1711
Cdd:TIGR02169 314 ----ERELEDAEERLAKLEAEIDKLLAEIEELE-----------------------------REIEEERKRRDKLTEEYa 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1712 --QTVRALAERKAEGVLAAQARA-----------EQLRDEaRDLLQAAQDKLQ-RLQELEGTYEENERALEGKAAQLDGL 1777
Cdd:TIGR02169 361 elKEELEDLRAELEEVDKEFAETrdelkdyreklEKLKRE-INELKRELDRLQeELQRLSEELADLNAAIAGIEAKINEL 439
|
330
....*....|.
gi 31982223 1778 EARMRSVLQAI 1788
Cdd:TIGR02169 440 EEEKEDKALEI 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1204-1571 |
1.66e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1204 DLAARTRRLEQWAQELQQTgvLGAFESSFLNMQGKLGMVQAIMSARNASAASTAKLVEAtegLRHEIGKTTERLTQLEAE 1283
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA--LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR---LEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1284 LTAVQDENFNANHALSGLERDGLALNLTLRQLDQhlEILKHSNFLGAYDS-IRHAHSQSTEAERRANASTFAVPSPVSNS 1362
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEA--QIEQLKEELKALREaLDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1363 ADTRRRTEVLmgaqkenfnrqhlanQQALGRLSAHAhtLSLTG-INELvcgapgdapcatspcggagcrdedgqprcggl 1441
Cdd:TIGR02168 834 AATERRLEDL---------------EEQIEELSEDI--ESLAAeIEEL-------------------------------- 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1442 GCSGAAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVK 1521
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1522 DFLSQEGAdpDSIEMVATRVLDisIPASPEQIQRLASEIAERVRSLADVD 1571
Cdd:TIGR02168 943 ERLSEEYS--LTLEEAEALENK--IEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1453-1753 |
2.72e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.29 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1453 ALGRARHTQAELQRALVEGGGILSRVSETR----RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEG 1528
Cdd:pfam07888 88 ELRQSREKHEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1529 ADPDSiemvaTRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHR--------------A 1594
Cdd:pfam07888 168 EEEAE-----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleelrsL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1595 RSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVdtQNTEQTLQRVQERMAGAEKSLNSAGERAR-QLDALLEALKL 1673
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMAAQRDRTQAELHQARL--QAAQLTLQLADASLALREGRARWAQERETlQQSAEADKDRI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1674 KRAgnSLAASTAEETAGSAQSRAREAEKQL-REQVGDQYQ---TVRALAERKAeGVLAAQARAEQLRDEARDLLQAAQDK 1749
Cdd:pfam07888 321 EKL--SAELQRLEERLQEERMEREKLEVELgREKDCNRVQlseSRRELQELKA-SLRVAQKEKEQLQAEKQELLEYIRQL 397
|
....
gi 31982223 1750 LQRL 1753
Cdd:pfam07888 398 EQRL 401
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1475-1794 |
2.78e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 55.43 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELRELIQNVKdflsqegadpdsiemvatrvldisipasPEQIQ 1554
Cdd:COG3064 18 LEQAEAEKRAAAEAEQKAKE---EAEEERLAELEAKRQAEEEAREAK----------------------------AEAEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1555 RLASEIAERVRSLADVDTILAHTmgDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQR-----AQGAAQGAIWGA 1629
Cdd:COG3064 67 RAAELAAEAAKKLAEAEKAAAEA--EKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaeeeAKRKAEEERKAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1630 VVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVGD 1709
Cdd:COG3064 145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEA---ADTAAAAAAALAAAAAAAAADAALLALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1710 QYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAIN 1789
Cdd:COG3064 222 AARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSA 301
|
....*
gi 31982223 1790 LQVQI 1794
Cdd:COG3064 302 ALAAE 306
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
987-1033 |
2.84e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 2.84e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 31982223 987 CECSGNIDPmdPDACDPHTGQCLrCLHNTEGPHCGYCKPGFHGQAAR 1033
Cdd:cd00055 2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1446-1794 |
3.28e-07 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 55.03 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1525
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 QEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKA 1605
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1606 ETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEK-------SLNSAGER---ARQLDALLEALK--- 1672
Cdd:COG0840 176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgdltvriDVDSKDEIgqlADAFNRMIENLRelv 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1673 --LKRAGNSLAAStAEETAGSAQSRAREAEKQlREQVgdqyQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKL 1750
Cdd:COG0840 256 gqVRESAEQVASA-SEELAASAEELAAGAEEQ-AASL----EETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 31982223 1751 QRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQI 1794
Cdd:COG0840 330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDI 373
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-516 |
3.35e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 31982223 473 CQCNSRGTVPGSspCDSSSGTCFCKRLVTGHGCDRCLPGHWGLS 516
Cdd:smart00180 1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1266-1616 |
3.41e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1266 LRHEIGKTTERLTQLEAELTAVQDENFNANHALSGLERDGLALNLTLRQLDQHLEILKHSNFLGAyDSIRHAHSQSTEAE 1345
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1346 RRANASTfavpSPVSNSADTRRRTEVLMGAQK---ENFNRQHLANQQALGRLSAHAHTLSltginelvcgapGDAPCATS 1422
Cdd:TIGR02168 761 AEIEELE----ERLEEAEEELAEAEAEIEELEaqiEQLKEELKALREALDELRAELTLLN------------EEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1423 PCGGAGCRDEDGQPRCGGLGCSGAAATADLAlgRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAS 1502
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIE--SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1503 RGQVEQANQELRELIQNVKDFLSQEGADPDSIEMvatrvldisipaspeQIQRLASEIAERVRSLADVdtILAHtmgdVR 1582
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEV---------------RIDNLQERLSEEYSLTLEE--AEAL----EN 961
|
330 340 350
....*....|....*....|....*....|....*
gi 31982223 1583 RAEQLLQDAHRARSRAEGERQKAETVQ-AALEEAQ 1616
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNlAAIEEYE 996
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1483-1795 |
3.66e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 55.05 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1483 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQN--VKDFLSQEGADPDSIEMVAtrvldisipaspEQIQRLASEI 1560
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEerLAELEAKRQAEEEAREAKA------------EAEQRAAELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1561 AERVRSLADvdtilahtmgdvrrAEQLLQDAhrarsraegERQKAETVQAALEEAQRAQgAAQGAIWGAvvDTQNTEQTL 1640
Cdd:COG3064 73 AEAAKKLAE--------------AEKAAAEA---------EKKAAAEKAKAAKEAEAAA-AAEKAAAAA--EKEKAEEAK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1641 QRVQERMAG-AEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGS-AQSRAREAEKQLREQVGDQYQTVRALA 1718
Cdd:COG3064 127 RKAEEEAKRkAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAaAALVAAAAAAVEAADTAAAAAAALAAA 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1719 ERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIY 1795
Cdd:COG3064 207 AAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAA 283
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
878-925 |
4.02e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.12 E-value: 4.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 31982223 878 CVCNGRA---DECDTHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 925
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1582-1783 |
4.66e-07 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 52.72 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1582 RRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAaqgaiwgavvdtqnTEQTLQRVQERMAGAEKSLNSAGERA 1661
Cdd:pfam00261 43 RRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV--------------LENRALKDEEKMEILEAQLKEAKEIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1662 RQLDALLE--ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLReQVGDQYQTVRALAErkaegvlAAQARAEQLRDEA 1739
Cdd:pfam00261 109 EEADRKYEevARKLVVVEGDL--ERAEERAELAESKIVELEEELK-VVGNNLKSLEASEE-------KASEREDKYEEQI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 31982223 1740 RDLlqaaQDKLQrlqELEGTYEENERALEGKAAQLDGLEARMRS 1783
Cdd:pfam00261 179 RFL----TEKLK---EAETRAEFAERSVQKLEKEVDRLEDELEA 215
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1580-1786 |
4.81e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1580 DVRRAEQLLQDAHRARSRAEGERQKAETVQAA-----LEEAQRAQGAAQGAiwgavvdtqnteqtLQRVQERMAGAEKSL 1654
Cdd:TIGR02794 61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKeleqrAAAEKAAKQAEQAA--------------KQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1655 NSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQyqtvrALAERKAEGVlAAQARAEQ 1734
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK-----AEAEAKAKAE-EAKAKAEA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1735 LRDEARdllQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQ 1786
Cdd:TIGR02794 201 AKAKAA---AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1551-1789 |
5.37e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIA---ERVRSLADVDTILAHTMGDV----RRAEQLLQDAHRARSRAEGE---------------------- 1601
Cdd:pfam01576 159 ERISEFTSNLAeeeEKAKSLSKLKNKHEAMISDLeerlKKEEKGRQELEKAKRKLEGEstdlqeqiaelqaqiaelraql 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1602 RQKAETVQAAL---EEAQRAQGAAQGAIwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALK--LKRA 1676
Cdd:pfam01576 239 AKKEEELQAALarlEEETAQKNNALKKI-------RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKteLEDT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1677 GNSLAAS----TAEETAGSAQSRAREAEKQLRE-QVGD----QYQTVRALAE-----RKAEGVL--AAQA----RAEqLR 1736
Cdd:pfam01576 312 LDTTAAQqelrSKREQEVTELKKALEEETRSHEaQLQEmrqkHTQALEELTEqleqaKRNKANLekAKQAleseNAE-LQ 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1737 DEARDLLQAAQDKLQR-------LQELEGTYEENERALEGKAAQLDGLEARMRSVLQAIN 1789
Cdd:pfam01576 391 AELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1589-1772 |
5.91e-07 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 51.41 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1589 QDAHRARsraegERQKAETVQAAL-------EEAQRAQGAAQGAIWGAVVDTQNTEQ-------TLQRVQERMAGAEKSL 1654
Cdd:pfam05335 15 QEAKAAN-----DAQAAAAEAAARqvknqlaDKALQAAKAAEAALAGKQQIVEQLEQelreaeaVVQEESASLQQSQANA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1655 NSAGERARQLDALLEALKlkragNSLAAstAEETAGSAQSRAREAEKQLREQvgdqyqtvRALAErkaegvlAAQARAEQ 1734
Cdd:pfam05335 90 NAAQRAAQQAQQQLEALT-----AALKA--AQANLENAEQVAAGAQQELAEK--------TQLLE-------AAKKRVER 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 31982223 1735 LrdeARDLLQAAQDklqrlqelegtYEENERALEgKAA 1772
Cdd:pfam05335 148 L---QRQLAEARAD-----------LEKTKKAAY-KAA 170
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
877-922 |
6.59e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 6.59e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 31982223 877 PCVCNGRAD---ECDTHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 922
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1611-1773 |
8.92e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1611 ALEEAQRAQGAAQGAIWGAV-VDTQNTEQTLQRVQERMAGAEKS----LNSAGERARQL--DALLEALKLK----RAGNS 1679
Cdd:TIGR02794 22 SLYHSVKPEPGGGAEIIQAVlVDPGAVAQQANRIQQQKKPAAKKeqerQKKLEQQAEEAekQRAAEQARQKeleqRAAAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1680 LAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQD-KLQRLQELEG 1758
Cdd:TIGR02794 102 KAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKA 181
|
170
....*....|....*
gi 31982223 1759 TYEENERALEGKAAQ 1773
Cdd:TIGR02794 182 KAEAEAKAKAEEAKA 196
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1475-1788 |
9.54e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQ-ANQELRELiqnvkDFLSQEGADPDSiemvatrvldisipaspEQI 1553
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERmAMEREREL-----ERIRQEERKREL-----------------ERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1554 --QRLASEIaERVRSLADVDtilahtMGDVRRAEQLLQDAHRARSRA--EGERQKAETVQAALEEAQRAQ--GAAQgaiw 1627
Cdd:pfam17380 366 rqEEIAMEI-SRMRELERLQ------MERQQKNERVRQELEAARKVKilEEERQRKIQQQKVEMEQIRAEqeEARQ---- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1628 gavVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETagsaQSRAREAEKQLREQV 1707
Cdd:pfam17380 435 ---REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1708 GDQYQTVRALAERKAEGVLAAQARAEQLR--DEARDLLQAAQDKLQRLQELEGTYEENERalegkaaqLDGLEaRMRSVL 1785
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRReaEEERRKQQEMEERRRIQEQMRKATEERSR--------LEAME-REREMM 578
|
...
gi 31982223 1786 QAI 1788
Cdd:pfam17380 579 RQI 581
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1482-1733 |
9.64e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 53.45 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1482 RRQAEEAQQRAQAALdkanASRGQVEQANQELreliQNVKDFLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIA 1561
Cdd:PRK07735 12 KEAARRAKEEARKRL----VAKHGAEISKLEE----ENREKEKALPKNDDMTIE---------------EAKRRAAAAAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1562 ERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRA-EGERQKAETVQAALEE---AQRAQGAAQGAIWGAVVDTQNTE 1637
Cdd:PRK07735 69 AKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAaALAKQKREGTEEVTEEekaAAKAKAAAAAKAKAAALAKQKRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1638 QTLQRVQE-RMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEE-------TAGSAQSRAREAEKQLREQV-- 1707
Cdd:PRK07735 149 GTEEVTEEeEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEkakakakAAAAAKAKAAALAKQKASQGng 228
|
250 260
....*....|....*....|....*...
gi 31982223 1708 --GDQYQTVRALAERKAEGVLAAQARAE 1733
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1552-1786 |
1.02e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.99 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1552 QIQRLaSEIAERVRSLADvdTILAHTMGDVRRAEQL--LQDAHRA-RSRAEGERQK---AETVQAALEEA-----QRAQG 1620
Cdd:pfam07111 71 QLQEL-RRLEEEVRLLRE--TSLQQKMRLEAQAMELdaLAVAEKAgQAEAEGLRAAlagAEMVRKNLEEGsqrelEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1621 AAQGAIWGAvvdTQNTEQTLQRVQERMAGAEKSLNSagerarqldalleaLKLKRAGNSLAASTAEETAGSAQSRAREAE 1700
Cdd:pfam07111 148 LHQEQLSSL---TQAHEEALSSLTSKAEGLEKSLNS--------------LETKRAGEAKQLAEAQKEAELLRKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1701 KQLREQVgdqyQTVRALAERKAEGVL------AAQARAEQLRD------EARDLLQAAQDKLQ-RLQELEGTYEENERAL 1767
Cdd:pfam07111 211 EELEAQV----TLVESLRKYVGEQVPpevhsqTWELERQELLDtmqhlqEDRADLQATVELLQvRVQSLTHMLALQEEEL 286
|
250 260
....*....|....*....|...
gi 31982223 1768 EGKAAQLDGLEA----RMRSVLQ 1786
Cdd:pfam07111 287 TRKIQPSDSLEPefpkKCRSLLN 309
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1473-1754 |
1.06e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 52.03 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1473 GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegadpdsiemvATRVLdisipASPEQ 1552
Cdd:pfam06008 9 GALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK-----------ATQTL-----AKAQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1553 IQRLASEIAERVRSLADvdtilahtmgdvrRAEQLLQDAHRARSRAEGERQKAE-----TVQAALEEAQRAQGAAQGaiw 1627
Cdd:pfam06008 73 VNAESERTLGHAKELAE-------------AIKNLIDNIKEINEKVATLGENDFalpssDLSRMLAEAQRMLGEIRS--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1628 gavvdtQNTEQTLQRVQERMAGAEKSLNSAGERAR----QLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQL 1703
Cdd:pfam06008 137 ------RDFGTQLQNAEAELKAAQDLLSRIQTWFQspqeENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1704 REQvgdqyQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQ 1754
Cdd:pfam06008 211 LAN-----QANLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLLLQEID 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1553-1775 |
1.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1553 IQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAEtvqAALEEAQRAQGAAQgaiwgAVVD 1632
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE---EELEELEAELEELR-----EELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1633 TQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKlkragnslaasTAEETAGSAQSRAREAEKQLREQVGDQYQ 1712
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31982223 1713 TVRALAERKAEGVLAAQARAEQLRDEardlLQAAQDKLQRLQElEGTYEENERALEGKAAQLD 1775
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEE----LEEAQEELEELEE-ELEQLENELEAAALEERLK 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1543-1797 |
1.36e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1543 DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEE--AQRAQG 1620
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1621 A----AQGAIWGAVVDTQNTEQTLQRVQ--ERMAGAEKSLnsagerARQLDALLEALKLKRAgnslaasTAEETAGSAQS 1694
Cdd:COG3883 95 LyrsgGSVSYLDVLLGSESFSDFLDRLSalSKIADADADL------LEELKADKAELEAKKA-------ELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1695 RAREAEKQLREqvgdqyqtvraLAERKAEgvlaAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQL 1774
Cdd:COG3883 162 LKAELEAAKAE-----------LEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250 260
....*....|....*....|...
gi 31982223 1775 DGLEARMRSVLQAINLQVQIYNT 1797
Cdd:COG3883 227 AAAAAAAAAAAAAAAAAASAAGA 249
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1637-1781 |
1.66e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 48.76 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1637 EQTLQRVQERMAGAEKSLNSAGERARQLDAllealKLKRagnslaastAEETAGSAQSRAREAE---KQLREQvgdqyqt 1713
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEE-----ERRQ---------AEEEAERLEQKRQEAEeekERLEES------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1714 vralAERKAEgvlaaqaRAEQLRDEARdllqAAQDKLQRLQElegtyEENERALEGKAAQLDGLEARM 1781
Cdd:pfam20492 71 ----AEMEAE-------EKEQLEAELA----EAQEEIARLEE-----EVERKEEEARRLQEELEEARE 118
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
927-985 |
1.72e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 1.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 31982223 927 PCPCPeGPGSQRHfatSCHRDGYsqqiVCQCREGYTGLRCEACAPGHFGDPSKPGGrCQ 985
Cdd:cd00055 1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1589-1788 |
1.81e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1589 QDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALL 1668
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1669 EALKLKRAgnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVR------ALAERKAEGVLAAQARAEQLRDEARDL 1742
Cdd:COG4942 100 EAQKEELA----------ELLRALYRLGRQPPLALLLSPEDFLDAVRrlqylkYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31982223 1743 LQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAI 1788
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1625-1794 |
1.88e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1625 AIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEAL--KLKRAGNSLAA-----STAEETAGSAQSRAR 1697
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerRIAALARRIRAleqelAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1698 EAEKQLREQVGDQYQTVRALAER----------KAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERAL 1767
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180
....*....|....*....|....*..
gi 31982223 1768 EGKAAQLDGLEARMRSVLQAINLQVQI 1794
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKL 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1548-1775 |
2.13e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1548 ASPEQIQRLaseiaervRSLADVDT---ILAHTMGDVRRAEQLLQDahrarsRAEGERQKAETVQAALEEAQRAQGAAqg 1624
Cdd:COG1579 1 AMPEDLRAL--------LDLQELDSeldRLEHRLKELPAELAELED------ELAALEARLEAAKTELEDLEKEIKRL-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1625 aiwgavvdtqntEQTLQRVQERMAGAEKSLNSAGErARQLDAL---LEALKLKRAgnslaastaeetagsaqsrarEAEK 1701
Cdd:COG1579 65 ------------ELEIEEVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRIS---------------------DLED 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1702 QLREqvgdqyqtvralAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQ-RLQELEGTYEENERALEGKAAQLD 1775
Cdd:COG1579 111 EILE------------LMERIEELEEELAELEAELAELEAELEEKKAELDeELAELEAELEELEAEREELAAKIP 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1477-1742 |
2.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1477 RVSETRRQAEEA---QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVAtrvldisipaspEQI 1553
Cdd:PTZ00121 1558 KKAEEKKKAEEAkkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------------EEL 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1554 QRlaseiAERVRSlaDVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGaaqgaiwgavvDT 1633
Cdd:PTZ00121 1626 KK-----AEEEKK--KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-----------DE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1634 QNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSA-QSRAREAEKQLREQVGDQYQ 1712
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270
....*....|....*....|....*....|
gi 31982223 1713 TVRALAERKAEGVLAAQARAEqlrDEARDL 1742
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEE---DEKRRM 1794
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1446-1773 |
3.11e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.96 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLA--LGRARHTQAELQRALVEgggilsrvsETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV--K 1521
Cdd:COG3064 69 AELAAEAAkkLAEAEKAAAEAEKKAAA---------EKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKaeE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1522 DFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGE 1601
Cdd:COG3064 140 ERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLAL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1602 RQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGErarqldalLEALKLKRAGNSLA 1681
Cdd:COG3064 220 AVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSG--------LVVVAAALAGLAAA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1682 ASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERkAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYE 1761
Cdd:COG3064 292 AAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVR-GGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAE 370
|
330
....*....|..
gi 31982223 1762 ENERALEGKAAQ 1773
Cdd:COG3064 371 AAGALLLGKLAD 382
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1587-1780 |
3.20e-06 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 51.89 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1587 LLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAgAEKSLNSAGerarQLDA 1666
Cdd:PRK15374 13 YTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDA-AREKLSSEG----QLTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1667 LLEALKLKRAGNSLAASTAEETAGSAQsraREAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRDEARDLL 1743
Cdd:PRK15374 88 LLGKLMTLLGDVSLSQLESRLAVWQAM---IESQKEMGIQVSKEFQTALGEAQeatDLYEASIKKTDTAKSVYDAAEKKL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 31982223 1744 QAAQDKLQRLQELEGTYEENERALEGKAAqlDGLEAR 1780
Cdd:PRK15374 165 TQAQNKLQSLDPADPGYAQAEAAVEQAGK--EATEAK 199
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1475-1768 |
3.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQ--ELRELIQNVK-DFL--SQEGADPDSIEMVATRvldisipAS 1549
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKaDEAkkAEEAKKADEAKKAEEK-------KK 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1550 PEQIQRlASEI--AERVRSLADVDTILAHTMGDVRRAEQLLQdAHRAR-------------------SRAEGERQKAETV 1608
Cdd:PTZ00121 1548 ADELKK-AEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKK-AEEARieevmklyeeekkmkaeeaKKAEEAKIKAEEL 1625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1609 QAALEEAQRAQGAAQGAiwgaVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEET 1688
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1689 AGSAQSRAREAE-KQLREQVGDQYQTVRALAE---RKAEgvlAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENE 1764
Cdd:PTZ00121 1702 KKAEELKKKEAEeKKKAEELKKAEEENKIKAEeakKEAE---EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
....
gi 31982223 1765 RALE 1768
Cdd:PTZ00121 1779 AVIE 1782
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1634-1789 |
4.08e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1634 QNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLrEQVGD--QY 1711
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNnkEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1712 QtvrALAERKAegvlAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAIN 1789
Cdd:COG1579 92 E---ALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1585-1755 |
5.56e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 48.41 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1585 EQLLQDAHRARSRAEGERQKA-ETVQAALEEAqRAQGAAQGAIWGAVVdTQNTEQTLQRVQERMAGAEKSLNsageraRQ 1663
Cdd:pfam01442 18 EQLGPVAQELVDRLEKETEALrERLQKDLEEV-RAKLEPYLEELQAKL-GQNVEELRQRLEPYTEELRKRLN------AD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1664 LDALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVlaaqarAEQLRDEARDLL 1743
Cdd:pfam01442 90 AEELQEKLAPYGEE---LRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEV------QAQLSQRLQELR 160
|
170
....*....|..
gi 31982223 1744 QAAQDKLQRLQE 1755
Cdd:pfam01442 161 EKLEPQAEDLRE 172
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1550-1755 |
5.56e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 49.29 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1550 PEQIqrLASEIAERVRSLADVDTILAHTMGDV----RRAEQLLQDAHRARSRAE-----GERQKAEtvqAALEEAQRAQG 1620
Cdd:pfam04012 23 PEKM--LEQAIRDMQSELVKARQALAQTIARQkqleRRLEQQTEQAKKLEEKAQaaltkGNEELAR---EALAEKKSLEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1621 AAQGaiwgavvdtQNTEQTLQRVQErmAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE 1700
Cdd:pfam04012 98 QAEA---------LETQLAQQRSAV--EQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDSF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 31982223 1701 KQLREQVgdqyqtvralAERKAEGVLAAQARAEQLRDEARDLLQA----AQDKLQRLQE 1755
Cdd:pfam04012 167 ERIEEKI----------EEREARADAAAELASAVDLDAKLEQAGIqmevSEDVLARLKA 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1587-1789 |
5.84e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1587 LLQDAHRARSRAEGERQKAETVQAALEEAQRA--QGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQL 1664
Cdd:PRK11281 20 LCLSSAFARAASNGDLPTEADVQAQLDALNKQklLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1665 DALLEALKlkragNSLAASTAEETAGSAQsraREAEKQLREQVGDQYQTVRALA-------------ERKAEGVLAAQAR 1731
Cdd:PRK11281 100 QAELEALK-----DDNDEETRETLSTLSL---RQLESRLAQTLDQLQNAQNDLAeynsqlvslqtqpERAQAALYANSQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1732 AEQ--------------LRDEARDLLQA------AQDKLQRlQELEG-----TYEENERALegKAAQLDGLEaRMRSVLQ 1786
Cdd:PRK11281 172 LQQirnllkggkvggkaLRPSQRVLLQAeqallnAQNDLQR-KSLEGntqlqDLLQKQRDY--LTARIQRLE-HQLQLLQ 247
|
....
gi 31982223 1787 -AIN 1789
Cdd:PRK11281 248 eAIN 251
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1634-1791 |
5.94e-06 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 49.64 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1634 QNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALK---------LKRagnslaastAEETAGSAQSRAREAEKQlr 1704
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNrriqlleeeLER---------TEERLAEALEKLEEAEKA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1705 eqvGDQYQTVR-ALAERKAEG-----VLAAQAR-AEQLRDEARDLLQAAQDKLQRLQ-ELEGTyEENERALEGKAAQldg 1776
Cdd:pfam00261 73 ---ADESERGRkVLENRALKDeekmeILEAQLKeAKEIAEEADRKYEEVARKLVVVEgDLERA-EERAELAESKIVE--- 145
|
170
....*....|....*
gi 31982223 1777 LEARMRSVLQaiNLQ 1791
Cdd:pfam00261 146 LEEELKVVGN--NLK 158
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1512-1794 |
5.99e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1512 ELRELIQNVKDFLSQEGADpdsIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTM---GDVRRAEQL- 1587
Cdd:pfam12128 143 EYRSIIQNDRTLLGRERVE---LRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILeddGVVPPKSRLn 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1588 -------LQDaHRARSRAEGERQKAETVQAALEEAQRAQGAAQGaIWGAVVDTQNTEQTLQrvqERMAGAEKSLNSager 1660
Cdd:pfam12128 220 rqqvehwIRD-IQAIAGIMKIRPEFTKLQQEFNTLESAELRLSH-LHFGYKSDETLIASRQ---EERQETSAELNQ---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1661 arQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLR--EQVG-----------DQYQTVRALAERKAEGVLA 1727
Cdd:pfam12128 291 --LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGafLDADietaaadqeqlPSWQSELENLEERLKALTG 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1728 AQARAEQlRDEARDLLQAAQ--DKLQRL-QELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQI 1794
Cdd:pfam12128 369 KHQDVTA-KYNRRRSKIKEQnnRDIAGIkDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNE 437
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1447-1794 |
6.01e-06 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 51.35 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1447 AATADLALGRARHTQAELQRALvegggilsrvsETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1526
Cdd:COG2203 337 ADQAAIAIERARLYEALEAALA-----------ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1527 EGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAE 1606
Cdd:COG2203 406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1607 TVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAE 1686
Cdd:COG2203 486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1687 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERA 1766
Cdd:COG2203 566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645
|
330 340
....*....|....*....|....*...
gi 31982223 1767 LEGKAAQLDGLEARMRSVLQAINLQVQI 1794
Cdd:COG2203 646 LALALASLVLLRALLATELDLILDSSLL 673
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1551-1783 |
6.03e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIAERVRSLA-DVdtilahtmgdvrraeQLLQDAHRARSRAEGERQK---AETVQAALEEAQRAQGAAQGAI 1626
Cdd:PRK04863 789 EQLRAEREELAERYATLSfDV---------------QKLQRLHQAFSRFIGSHLAvafEADPEAELRQLNRRRVELERAL 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1627 WGAVVDTQNTEQTLQRVQERMAGAEKSL--------NSAGERARQLDALLEALK-----LKRAGNSL------AASTAEE 1687
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSALNRLLprlnlladETLADRVEEIREQLDEAEeakrfVQQHGNALaqlepiVSVLQSD 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1688 TAGSAQSRAR--EAEKQLReqvgDQYQTVRALAE----------RKAEGVLAA-----------QARAEQLRDEARDLLQ 1744
Cdd:PRK04863 934 PEQFEQLKQDyqQAQQTQR----DAKQQAFALTEvvqrrahfsyEDAAEMLAKnsdlneklrqrLEQAEQERTRAREQLR 1009
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1745 AAQDKL----QRLQELEGTYE-------ENERALEGKAAQLD-GLEARMRS 1783
Cdd:PRK04863 1010 QAQAQLaqynQVLASLKSSYDakrqmlqELKQELQDLGVPADsGAEERARA 1060
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1553-1754 |
6.40e-06 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 50.11 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1553 IQRLASEIAERVR---SLADVDTILAHTMGDVRRAEqlLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGA 1629
Cdd:pfam00529 31 VTRVLVKEGDRVKagdVLFQLDPTDYQAALDSAEAQ--LAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1630 VVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDallealklkragnslaasTAEETAGSAQSRAREAEKQLREQVGD 1709
Cdd:pfam00529 109 QAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLV------------------TAGALVAQAQANLLATVAQLDQIYVQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 31982223 1710 QYQTVRALAERKAEGVLAAQARAEQLRDEardlLQAAQDKLQRLQ 1754
Cdd:pfam00529 171 ITQSAAENQAEVRSELSGAQLQIAEAEAE----LKLAKLDLERTE 211
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1476-1789 |
6.52e-06 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 49.66 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1476 SRVSETRRQAEEAQQRAqAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvATRVLDISIPASPEQIQR 1555
Cdd:COG4223 7 AAVAELPAQLTALEQRL-AALEAAPAAAAATAALEARLAAL---------------------RAALAAAREAVAAAAAAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1556 LASEIAErvrsladvdtilahtmgdvrraeqlLQDAHRARSRAEGERQKAETVQAALEEAQRAqgAAQGAIWGAVVDT-Q 1634
Cdd:COG4223 65 LEARLAA-------------------------LEAKAAAPEAEAAAAARAAALALAAAALRAA--VERGQPFAAELAAlE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1635 NTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALklkragnsLAASTAEETAGSAQSRAREAekqLREQVgdqyqTV 1714
Cdd:COG4223 118 ALAPDAPALAALAAFAATGVPTLAALRAEFPAAARAA--------LAAARAPEADASWLDRLLAF---ARSLV-----TV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1715 RALAERKAEGVLAAQARAEQLRDEARdlLQAAqdklqrLQELEgtyeenerALEGKAAQ-----LDGLEARMRsVLQAIN 1789
Cdd:COG4223 182 RRVGPVEGDDPDAILARAEAALAAGD--LAGA------LAELE--------ALPEAAQAaaapwIAKAEARLA-ADAALQ 244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1588-1779 |
7.30e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1588 LQDAHRARSRAEGERQKAETVQAalEEAQRAQGAAQGAIwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLdal 1667
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQA--EELQQKQAAEQERL-------KQLEKERLAAQEQKKQAEEAAKQAALKQKQA--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1668 lEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTV-----RALAERKAEGVLAAQARAEQLRDEARDL 1742
Cdd:PRK09510 135 -EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAaeakkKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
170 180 190
....*....|....*....|....*....|....*..
gi 31982223 1743 LQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEA 1779
Cdd:PRK09510 214 EAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1552-1716 |
7.47e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1552 QIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGErqkAETVQAALEEAQRAQG---------AA 1622
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGnvrnnkeyeAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1623 QGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAgNSLAASTAEETAgsAQSRAREAEKQ 1702
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEE--LEAEREELAAK 171
|
170
....*....|....
gi 31982223 1703 LREQVGDQYQTVRA 1716
Cdd:COG1579 172 IPPELLALYERIRK 185
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1462-1774 |
7.85e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1462 AELQRALVEGGGILSRVSETRRQaeEAQQRAQAALDKANAS-RGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATR 1540
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1541 VLDISIP---ASPEQIQRLASEIAERVRSLAdvdtILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETvQAALEEAQR 1617
Cdd:pfam12128 334 FLDADIEtaaADQEQLPSWQSELENLEERLK----ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL-AKIREARDR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1618 AQGAAQGAIwgavvdtqntEQTLQRVQERMAGAEKSLNsagERARQLDALLEALKLKragnsLAASTAEETAGSAQSRAR 1697
Cdd:pfam12128 409 QLAVAEDDL----------QALESELREQLEAGKLEFN---EEEYRLKSRLGELKLR-----LNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1698 EAEKQLREQVGDQYQTVRALAErkaegvlaAQARAEQLRDEARDLLQAAQdklQRLQELEGTYEENERALEGKAAQL 1774
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQS--------ELRQARKRRDQASEALRQAS---RRLEERQSALDELELQLFPQAGTL 536
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1594-1748 |
8.31e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 50.64 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1594 ARSRAEGERQKAETVQAALEEAQRAQGAAQgaiwgavvdtqnteqtlqRVQERMAGAEKSLNSAGERArqlDAllealKL 1673
Cdd:PRK12472 188 APARAETLAREAEDAARAADEAKTAAAAAA------------------REAAPLKASLRKLERAKARA---DA-----EL 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1674 KRAGNSLAASTAEETAGSAQSRAREAEKQLREqVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQD 1748
Cdd:PRK12472 242 KRADKALAAAKTDEAKARAEERQQKAAQQAAE-AATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATD 315
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1532-1719 |
1.15e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 47.64 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1532 DSIEMVATRVLDISipaspEQIQRLASEIAERV-RSLADVDTILAHTMGDVR-RAEQLLQDAH-RARSRAEGERQKAETV 1608
Cdd:pfam01442 4 DSLDELSTYAEELQ-----EQLGPVAQELVDRLeKETEALRERLQKDLEEVRaKLEPYLEELQaKLGQNVEELRQRLEPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1609 QAALEEAQRaqgaaqgaiwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERAR-QLDALLEALKLK-----RAGNSLAA 1682
Cdd:pfam01442 79 TEELRKRLN----------------ADAEELQEKLAPYGEELRERLEQNVDALRaRLAPYAEELRQKlaerlEELKESLA 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 31982223 1683 STAEEtagsAQSRAREAEKQLREQVGDQYQTVRALAE 1719
Cdd:pfam01442 143 PYAEE----VQAQLSQRLQELREKLEPQAEDLREKLD 175
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1585-1779 |
1.18e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 48.95 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1585 EQLLQDAHRARSRAEGERQKAETVQAALEEA-QRAQGAAQgAIWGAVVDTQN-TEQTLQRVQERMAGAEKSLNSAGERAr 1662
Cdd:pfam06008 50 SSLAQETEELQKKATQTLAKAQQVNAESERTlGHAKELAE-AIKNLIDNIKEiNEKVATLGENDFALPSSDLSRMLAEA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1663 qlDALLEALKLKRAGNSLAASTAEetagsaqsrAREAEKqLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDL 1742
Cdd:pfam06008 128 --QRMLGEIRSRDFGTQLQNAEAE---------LKAAQD-LLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLREL 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 31982223 1743 LQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEA 1779
Cdd:pfam06008 196 LREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKN 232
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
954-984 |
1.25e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.88 E-value: 1.25e-05
10 20 30
....*....|....*....|....*....|.
gi 31982223 954 VCQCREGYTGLRCEACAPGHFGDPSKPGGRC 984
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1552-1794 |
1.26e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1552 QIQRLAS-EIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAE----------GERQKA-ETVQAALEEAQRAQ 1619
Cdd:COG3206 86 QIEILKSrPVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGsnvieisytsPDPELAaAVANALAEAYLEQN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1620 GAAQgaiwgavvdTQNTEQTLQRVQERMAGAEKSLNSAgERArqldalLEALKLKRAGNSLaastaEETAGSAQSRAREA 1699
Cdd:COG3206 166 LELR---------REEARKALEFLEEQLPELRKELEEA-EAA------LEEFRQKNGLVDL-----SEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1700 EKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEA-RDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLE 1778
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
250
....*....|....*.
gi 31982223 1779 ARMRSVLQAINLQVQI 1794
Cdd:COG3206 305 AQLQQEAQRILASLEA 320
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1446-1745 |
1.26e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.82 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1446 AAATADLAlgrarhTQAELQRALVEGggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1525
Cdd:smart00283 17 AEELEELA------ERMEELSASIEE--VAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1526 QEgadpDSIEMVATRVLDISipaspEQIQRLA-----------------SEIAERVRSLADvdtilahtmgdvrraeqll 1588
Cdd:smart00283 89 SS----DEIGEIVSVIDDIA-----DQTNLLAlnaaieaarageagrgfAVVADEVRKLAE------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1589 qdahraRSRAEgerqkAETVQAALEEAQRAQGAAQGAIWGAvvdTQNTEQTLQRVQErmagAEKSLNSAGERARQLDALL 1668
Cdd:smart00283 141 ------RSAES-----AKEIESLIKEIQEETNEAVAAMEES---SSEVEEGVELVEE----TGDALEEIVDSVEEIADLV 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1669 EalklkragnSLAASTAEETAGSaqsrareaekqlrEQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQA 1745
Cdd:smart00283 203 Q---------EIAAATDEQAAGS-------------EEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1461-1782 |
1.36e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1461 QAELQRALVEgggilsrvsETRRQAEEAQQRAQAALDKAnASRGQVEQANQELReliqnvkdflsqegADpdsiemvatr 1540
Cdd:COG3064 38 EAEEERLAEL---------EAKRQAEEEAREAKAEAEQR-AAELAAEAAKKLAE--------------AE---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1541 vldisipASPEQIQRLASEIAERVRsladvdtilahtmgdvRRAEQLLQDAhRARSRAEGE-----RQKAEtvQAALEEA 1615
Cdd:COG3064 84 -------KAAAEAEKKAAAEKAKAA----------------KEAEAAAAAE-KAAAAAEKEkaeeaKRKAE--EEAKRKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1616 QRAQGAAQGAIWGAvvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSR 1695
Cdd:COG3064 138 EEERKAAEAEAAAK----AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1696 AREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLD 1775
Cdd:COG3064 214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
....*..
gi 31982223 1776 GLEARMR 1782
Cdd:COG3064 294 GLVLDDS 300
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1546-1701 |
1.55e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 49.48 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1546 IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEgerqkaetvqAALEEAQRAQGAAQga 1625
Cdd:PRK12472 185 LAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARAD----------AELKRADKALAAAK-- 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1626 iwgavvdtqnTEQTLQRVQERMAgaeKSLNSAGERARQLDALLEALKLKRAgnslAASTAEETAGSAQSRAREAEK 1701
Cdd:PRK12472 253 ----------TDEAKARAEERQQ---KAAQQAAEAATQLDTAKADAEAKRA----AAAATKEAAKAAAAKKAETAK 311
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
987-1029 |
1.60e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.45 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 31982223 987 CECS--GNIDPmdpdACDPHTGQCLrCLHNTEGPHCGYCKPGFHG 1029
Cdd:smart00180 1 CDCDpgGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1502-1736 |
1.63e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 49.08 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1502 SRGQVEQANQELreliqNVKDFLSQEGADP-------DSIE--------MVATR------VLDISIPA-SPEQiqrlASE 1559
Cdd:COG3524 84 SRDAVERLDAEL-----DLRAHYSRPGIDPlsrldpdASIEdlykyyrrRVKVEydstsgIITLEVRAfDPED----AQA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1560 IAERVRSLAD--VDTILAhtmgdvRRAEQLLQDAHRARSRAEGERQKAetvQAALEEAQRAQG----AAQGAIWGAVVdt 1633
Cdd:COG3524 155 IAEALLAESEelVNQLSE------RAREDAVRFAEEEVERAEERLRDA---REALLAFRNRNGildpEATAEALLQLI-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1634 QNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEAL-----KLKR------AGNSLAASTAE-ETAgsaqsrarEAEK 1701
Cdd:COG3524 224 ATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALekqiaAERArltgasGGDSLASLLAEyERL--------ELER 295
|
250 260 270
....*....|....*....|....*....|....*
gi 31982223 1702 QLREQvgdQYQTVRALAErkaegvlaaQARAEQLR 1736
Cdd:COG3524 296 EFAEK---AYTSALAALE---------QARIEAAR 318
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1575-1768 |
1.70e-05 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 48.75 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1575 AHTMGDVRRAEQLLQdahRARSRAEGERQKAETVQAaleEAQRAQGAAQGAIwgAVVDtqnteqTLQRVQERMAGAEKSL 1654
Cdd:COG3071 60 AQALGDYERRDEYLA---QALELAPEAELAVLLTRA---ELLLDQGQAEQAL--ATLE------ALRAGAPRHPQVLRLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1655 NSAGERARQLDALLEAL-KLKRAGnslaASTAEEtagsAQSRAREAEKQLREQVGDQYQTVRAL------AERKAEGVLA 1727
Cdd:COG3071 126 LQAYRQLGDWEELLELLpALRKHK----ALSAEE----AQALERRAYLGLLRQAARDAEALKALwkalprAERRDPELAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1728 AQARA-EQLRD--EARDLLQAAQDK------LQRLQELEGtyEENERALE 1768
Cdd:COG3071 198 AYARAlIALGDhdEAERLLREALKRqwdprlVRLYGRLQG--GDPAKQLK 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1243-1681 |
1.74e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1243 QAIMSARNASAASTAKLVEategLRHEIGKTTERLTQLEAELTAVQDENFNANHAL---SGLERDGLALNLTLRQLDQHL 1319
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVE----MARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1320 EILKHsnflgaydsirhAHSQSTEAERRANASTFAVPSPVSNSADTRRRTEVLmgaQKENfnrqhLANQQALGRLsAHAH 1399
Cdd:PRK04863 369 EVVEE------------ADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQ---QTRA-----IQYQQAVQAL-ERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1400 TLsltginelvCGAPGDAPcatspcGGAGCRDEDGQPRcgglgcSGAAATADLALG---------RARHTQA-ELQRALv 1469
Cdd:PRK04863 428 QL---------CGLPDLTA------DNAEDWLEEFQAK------EQEATEELLSLEqklsvaqaaHSQFEQAyQLVRKI- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1470 eGGGIlsrvsetrrQAEEAQQRAQAALDKANASR---GQVEQANQELRELIQNVKDFLSQEGAdPDSIEMVATRVLDisi 1546
Cdd:PRK04863 486 -AGEV---------SRSEAWDVARELLRRLREQRhlaEQLQQLRMRLSELEQRLRQQQRAERL-LAEFCKRLGKNLD--- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1547 paSPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRA-EQLLQDAHRARSRAegerQKAETVQAALEEAQRAQGAAQGa 1625
Cdd:PRK04863 552 --DEDELEQLQEELEARLESLSESVSEARERRMALRQQlEQLQARIQRLAARA----PAWLAAQDALARLREQSGEEFE- 624
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1626 iwgavvDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALkLKRAGNSLA 1681
Cdd:PRK04863 625 ------DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL-SQPGGSEDP 673
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1477-1793 |
1.84e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1477 RVSETRRQAEE-AQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQR 1555
Cdd:COG3064 121 KAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1556 LASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAE--GERQKAETVQAALEEAQRAQGAAQGAIWGAVVDT 1633
Cdd:COG3064 201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAlgGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1634 QNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSL-----AASTAEETAGSAQSRAREAEK------Q 1702
Cdd:COG3064 281 VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALvvrggGAASLEAALSLLAAGAAAAAAgagalaT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1703 LREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMR 1782
Cdd:COG3064 361 GALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKL 440
|
330
....*....|.
gi 31982223 1783 SVLQAINLQVQ 1793
Cdd:COG3064 441 VADLAGGLVGI 451
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-338 |
1.93e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.50 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055 2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1475-1770 |
2.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQAEEAQQRAQAaLDKANASRGQVEQAnQELRELIQNVKDFLSQEGADPDSIEmvATRVLDISIPASPEQIQ 1554
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEA-KKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1555 RLASEIAERVRSLADvdtilahtmgDVRRAEQLLQDAHRARsRAEgERQKAETVQAAlEEAQRAQGAAQGAIWGAVVDTQ 1634
Cdd:PTZ00121 1486 DEAKKKAEEAKKKAD----------EAKKAAEAKKKADEAK-KAE-EAKKADEAKKA-EEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1635 NTEQTLQ----RVQERMAGAEKSLNSAGERARQLDALLEalklKRAGNSLAASTAEETAGSAQSRAREAEKQLREQV--- 1707
Cdd:PTZ00121 1553 KAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEE----ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkka 1628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1708 ------GDQYQTVRALAERKAEGVLAAQ----ARAEQLR-------DEARDLLQAAQDKLQRLQELEGTYEENERALEGK 1770
Cdd:PTZ00121 1629 eeekkkVEQLKKKEAEEKKKAEELKKAEeenkIKAAEEAkkaeedkKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
928-977 |
2.74e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 2.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31982223 928 CPCPEGpgsqRHFATSCHRDGYsqqiVCQCREGYTGLRCEACAPGHFGDP 977
Cdd:smart00180 1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1582-1795 |
2.80e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1582 RRAEQLLQDA----HRARSRAEGERQKAETVQAALEEAQRAqgaaqgaiwgavVDTQNTEQTLQRVQERMAgaEKSLNsa 1657
Cdd:pfam13868 91 EEYEEKLQEReqmdEIVERIQEEDQAEAEEKLEKQRQLREE------------IDEFNEEQAEWKELEKEE--EREED-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1658 gER----ARQLDALLEALKLKRAgnslaastaeetagsAQSRAREAEKQ-LREQvgdQYQTVRALAERkaEGVLAAQARA 1732
Cdd:pfam13868 155 -ERileyLKEKAEREEEREAERE---------------EIEEEKEREIArLRAQ---QEKAQDEKAER--DELRAKLYQE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1733 EQLRDEARDLLQAAQDKLQRLQELEGTYEE----NERALEgKAAQLDglEARMRSVLQAINLQVQIY 1795
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEqielKERRLA-EEAERE--EEEFERMLRKQAEDEEIE 277
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1477-1787 |
2.99e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1477 RVSETRRQAEEAQQR-AQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-IQ 1554
Cdd:PRK04863 787 RIEQLRAEREELAERyATLSFDV------------QKLQRLHQAFSRFIGSH--------------LAVAFEADPEAeLR 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1555 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRA-----EGERQKAETVQAALEEAQRA------QGAAQ 1623
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladETLADRVEEIREQLDEAEEAkrfvqqHGNAL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1624 GAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLE---ALKLKRAGNSLAASTA--------EETAGSA 1692
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrraHFSYEDAAEMLAKNSDlneklrqrLEQAEQE 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1693 QSRAREAEKQLREQVgDQYQTVRA------------LAERKAE----GVLA---AQARAEQLRDEARDLLQAAQDKLQRL 1753
Cdd:PRK04863 1001 RTRAREQLRQAQAQL-AQYNQVLAslkssydakrqmLQELKQElqdlGVPAdsgAEERARARRDELHARLSANRSRRNQL 1079
|
330 340 350
....*....|....*....|....*....|....*.
gi 31982223 1754 QELEGTYEENERALEGK--AAQLDGLEARmRSVLQA 1787
Cdd:PRK04863 1080 EKQLTFCEAEMDNLTKKlrKLERDYHEMR-EQVVNA 1114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1450-1594 |
3.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1450 ADLALGRARHTQAELQ---RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1526
Cdd:COG4913 659 DEIDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1527 --EGADPDSIEMVATRVLDISIPASPEQIQRlasEIAERVRSLAdvdtilahtmGDVRRAEQLLQDAHRA 1594
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE---NLEERIDALR----------ARLNRAEEELERAMRA 795
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
350-401 |
3.14e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.73 E-value: 3.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 350 CECNGH---THSCHFdmavylasgnvSGGVCDgCQHNTAGRHCEFCRPFFYRDPT 401
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1580-1782 |
3.48e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1580 DVRRAEQLLQDAH----RARSRAEGERQKAETVQAALEEAQRAQGAAQGAIwgavvDTQNtEQTLQRVQERMAGAEKSLN 1655
Cdd:pfam13868 7 ELRELNSKLLAAKcnkeRDAQIAEKKRIKAEEKEEERRLDEMMEEERERAL-----EEEE-EKEEERKEERKRYRQELEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1656 --SAGERARQLDA---LLEALKLKRAgnsLAASTAEETAgsAQSRAREAEKQLREQVgDQYQtvRALAERKaegvlaaQA 1730
Cdd:pfam13868 81 qiEEREQKRQEEYeekLQEREQMDEI---VERIQEEDQA--EAEEKLEKQRQLREEI-DEFN--EEQAEWK-------EL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1731 RAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMR 1782
Cdd:pfam13868 146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
1661-1779 |
3.50e-05 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 45.73 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1661 ARQLDALLEALKLKRAGNSLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRD 1737
Cdd:pfam16535 1 AGQLTLLLGNLMSLLGEVSLSQLESRIAAWKAMQ---EAQQQKGLELSDEFQTALSEAEeatDAYEKAINKLKNAKSKAK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 31982223 1738 EARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEA 1779
Cdd:pfam16535 78 AAEKKIDQAQTRLQSLAPDSPGKAKLEAAEQQAGIKKDALQA 119
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
350-402 |
3.87e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 42.73 E-value: 3.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 350 CECNGH---THSCHFDmavylasgnvsGGVCDgCQHNTAGRHCEFCRPFFYRDPTK 402
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
1562-1796 |
6.63e-05 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 46.62 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1562 ERVRSLADVDTILaHTMGDVRRA----EQLLQDAHRARSRAEGERQKAETVQAAL------EEAQRAQGAAQgaiwgAVV 1631
Cdd:pfam16591 3 ERSDRMTDISQLN-DTLTDLRIArlqyMLSNGDATAAQAVQKKLDELKQQLQQLKttftspENVRLLQEQLQ-----LIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1632 DTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEAlklkRAGNSLAASTAEETAGSAQSRAREAEKQLREQV-GDQ 1710
Cdd:pfam16591 77 AYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEA----EVLQTPEADSRRAAQYQAISELKRQVQMARYQVrGYT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1711 YQTVRALAERKAEGVLAAQARAEQLRDeardllQAAQDKLQRLQELegtyeenERALEGKAAQLDGLEARMRSVLQA-IN 1789
Cdd:pfam16591 153 FTPNEDSEQAAYQQLDAALASLDQLRQ------ALAGDPGAALQQL-------TSALQGYRDALDTFKAAVAAIEQArQE 219
|
....*..
gi 31982223 1790 LQVQIYN 1796
Cdd:pfam16591 220 MTSQGDE 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1638-1788 |
6.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1638 QTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAgnSLAASTAEETAgsAQSRAREAEKQLreQVGDQYQTVRAL 1717
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE--ELEELEAELEE--LREELEKLEKLL--QLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1718 AERKAEGvlaaQARAEQLRDEARDL------LQAAQDKLQRLQE-----LEGTYEENERALEGKAAQLDGLEARMRSVLQ 1786
Cdd:COG4717 138 EAELAEL----PERLEELEERLEELreleeeLEELEAELAELQEeleelLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
..
gi 31982223 1787 AI 1788
Cdd:COG4717 214 EL 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1548-1760 |
7.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1548 ASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAEtVQAALEEAQRAqgaaqgaiw 1627
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE-LPERLEELEER--------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1628 gavvdtqntEQTLQRVQERMAGAEKSLNsagERARQLDALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREqv 1707
Cdd:COG4717 155 ---------LEELRELEEELEELEAELA---ELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEE-- 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 31982223 1708 gdqyqtvralAERKAEgvlAAQARAEQLRDEARdllqaAQDKLQRLQELEGTY 1760
Cdd:COG4717 218 ----------AQEELE---ELEEELEQLENELE-----AAALEERLKEARLLL 252
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1645-1774 |
8.07e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1645 ERMAGAEKSLNSAGeraRQLDALLEALKLKRAGN-SLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAERKAE 1723
Cdd:PRK09039 46 REISGKDSALDRLN---SQIAELADLLSLERQGNqDLQDSVANLRASLSAA---EAERSRLQALLAELAGAGAAAEGRAG 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1724 GVLAAQARAEQLRDEAR---DLLQ----AAQDKLQRLQELEGTYEENERALEGKAAQL 1774
Cdd:PRK09039 120 ELAQELDSEKQVSARALaqvELLNqqiaALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1475-1619 |
1.02e-04 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 44.31 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETR-RQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvatrvldisipaSPEQI 1553
Cdd:pfam07321 4 LLRVKHLReDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAW--------------------------------RPQEE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1554 QRLASEIAERVRSLADVDTILaHTMGDVRRAEQLL-QDAHRARSRAEGERQKAETVQAALEEAQRAQ 1619
Cdd:pfam07321 52 QRLYAEIQGKLVLLKELEKVK-QQVALLRENEADLeKQVAEARQQLEAEREALRQARQALAEARRAV 117
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1489-1783 |
1.20e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1489 QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE----M--VATR---VLDISIPASPEQIQ---RL 1556
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRdlkdMldVKERkinVLQKKIENLQEQLRdkdKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1557 ASEIAERVRSL----ADVDTILAhTMgdvrraEQLLQDAHRARSRAEGERQKAEtvQAALEEAQRAQGaaqgaiwgavvD 1632
Cdd:pfam10174 417 LAGLKERVKSLqtdsSNTDTALT-TL------EEALSEKERIIERLKEQRERED--RERLEELESLKK-----------E 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1633 TQNTEQTLQRVQERMAGAEKSLNSAGERARQL--DALLEALKLKRAGNSLAASTAEETAGSAQS-RAREAEKQLR--EQV 1707
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLkKAHNAEEAVRtnPEI 556
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1708 GDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRS 1783
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1697-1793 |
1.25e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1697 REAEKQL---REQVGDQyQTVRALAERKAEgvlAAQARAEQLRDEARDLLQAAQDKL-----QRLQELEGTYEENERALE 1768
Cdd:COG1842 33 RDMEEDLveaRQALAQV-IANQKRLERQLE---ELEAEAEKWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA 108
|
90 100
....*....|....*....|....*
gi 31982223 1769 gkaaQLDGLEARMRSVLQAINLQVQ 1793
Cdd:COG1842 109 ----QLEEQVEKLKEALRQLESKLE 129
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1530-1774 |
1.46e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1530 DPDSIEMVATRV-LDISIPASPEQ-----IQRLASE-----IAERVRSLADVDTILAHTmgDVRRAEQLLQDAHRARSRA 1598
Cdd:TIGR02794 44 DPGAVAQQANRIqQQKKPAAKKEQerqkkLEQQAEEaekqrAAEQARQKELEQRAAAEK--AAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1599 EGERQKAETVQAALEEAQRAQGAAQGAIWGAvvdtqntEQtlQRVQERMAGAEKslnSAGERARQLDAllEALKLKRAGN 1678
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQA-------EE--EAKAKAAAEAKK---KAEEAKKKAEA--EAKAKAEAEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1679 SLAASTAEETAGSAQSRAR-EAEKqlreqvgdqyqtvRALAERKAEGVLAAQARAEQLrdEARDLLQAAQDKLQRLQElE 1757
Cdd:TIGR02794 188 KAKAEEAKAKAEAAKAKAAaEAAA-------------KAEAEAAAAAAAEAERKADEA--ELGDIFGLASGSNAEKQG-G 251
|
250
....*....|....*..
gi 31982223 1758 GTYEENERALEGKAAQL 1774
Cdd:TIGR02794 252 ARGAAAGSEVDKYAAII 268
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1551-1780 |
1.52e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIAERVRSLADVDTIlahtmgDVRRAEQLLQDAHRARSrAEGERQKAETVQAALEE---AQRAQGAAQGAIW 1627
Cdd:PRK07735 32 AEISKLEEENREKEKALPKNDDM------TIEEAKRRAAAAAKAKA-AALAKQKREGTEEVTEEekaKAKAKAAAAAKAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1628 GAVVDTQNTEQTLQRVQERMAGAEKSlnsAGERARQLDAllEALKLKRAGNSLAASTAEET-----------AGSAQSRA 1696
Cdd:PRK07735 105 AAALAKQKREGTEEVTEEEKAAAKAK---AAAAAKAKAA--ALAKQKREGTEEVTEEEEETdkekakakaaaAAKAKAAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1697 REAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAeqlrdeardllqAAQDKLQRLQELEGTYEENER-----ALEGKA 1771
Cdd:PRK07735 180 LAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKA------------AALAKQKASQGNGDSGDEDAKakaiaAAKAKA 247
|
....*....
gi 31982223 1772 AQLDGLEAR 1780
Cdd:PRK07735 248 AAAARAKTK 256
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
1682-1793 |
1.62e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 44.16 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1682 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARDLLQAAQDKLQRLQELE 1757
Cdd:PRK14475 36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 31982223 1758 GTYEENERALEGKAAQLDgLEARMRSVLQAINLQVQ 1793
Cdd:PRK14475 115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1686-1793 |
1.64e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1686 EETAGSAQSRAR--EAEKQLRE-------------QVGDQYQTvraLaERKAEgvlaaQA-RAEQLRDEARDL---LQAA 1746
Cdd:COG1196 162 EEAAGISKYKERkeEAERKLEAteenlerledilgELERQLEP---L-ERQAE-----KAeRYRELKEELKELeaeLLLL 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 31982223 1747 QDKL--QRLQELEGTYEENERALEGKAAQLDGLEAR---MRSVLQAINLQVQ 1793
Cdd:COG1196 233 KLREleAELEELEAELEELEAELEELEAELAELEAEleeLRLELEELELELE 284
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1453-1724 |
1.67e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1453 ALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKdFLSQEgadpd 1532
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE-SLQEE----- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1533 sIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQllqdahRARSRAEGERQKAETVQAAL 1612
Cdd:COG4372 166 -LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE------ELLEAKDSLEAKLGLALSAL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1613 EEAQRAQGAAQGAIWGAVVDtQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSA 1692
Cdd:COG4372 239 LDALELEEDKEELLEEVILK-EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
250 260 270
....*....|....*....|....*....|..
gi 31982223 1693 QSRAREAEKQLREQVGDQYQTVRALAERKAEG 1724
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVG 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1451-1686 |
1.68e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1451 DLALGRARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegad 1530
Cdd:COG1579 16 DSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1531 pdsiemvatrvldISipaSPEQIQRLASEIAervrSLAdvdtilahtmgdvRRAEQLLQDAHRARSRAEGERQKAETVQA 1610
Cdd:COG1579 85 -------------VR---NNKEYEALQKEIE----SLK-------------RRISDLEDEILELMERIEELEEELAELEA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1611 ALEEAQRAQGAAQGAIWGAVVDtqnTEQTLQRVQERMAGAEKSLNsagerarqlDALLEA-LKLKRAGNSLAASTAE 1686
Cdd:COG1579 132 ELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKIP---------PELLALyERIRKRKNGLAVVPVE 196
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1475-1787 |
1.74e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1475 LSRVSETRRQA-------EEAQQRAQAA-LDKANASRGQVEQANQELRELIQNVKDFLSQEgadpdsiemvatrvldisi 1546
Cdd:COG3096 245 LEAIRVTQSDRdlfkhliTEATNYVAADyMRHANERRELSERALELRRELFGARRQLAEEQ------------------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1547 paspEQIQRLASEIAERVRSLADVDTilahtmgDVRRAE---QLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQ 1623
Cdd:COG3096 306 ----YRLVEMARELEELSARESDLEQ-------DYQAASdhlNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1624 GAIWGAVVDTQNTEQTLQR-------------VQERMAGAEKSLNSAGERARQLDAlLEALKLKRAGNSLAASTAEETAg 1690
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSlksqladyqqaldVQQTRAIQYQQAVQALEKARALCG-LPDLTPENAEDYLAAFRAKEQQ- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1691 sAQSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQA--RAEQLRDEARDLlqaaQDKLQRLQELEGTYEENERA 1766
Cdd:COG3096 453 -ATEEVLELEQKLSvaDAARRQFEKAYELVCKIAGEVERSQAwqTARELLRRYRSQ----QALAQRLQQLRAQLAELEQR 527
|
330 340
....*....|....*....|....
gi 31982223 1767 LEGKAA---QLDGLEARMRSVLQA 1787
Cdd:COG3096 528 LRQQQNaerLLEEFCQRIGQQLDA 551
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1692-1794 |
2.06e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1692 AQSRAREAEKQLrEQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARDLLQAAQDKL---QRLQELEGTYEENERALE 1768
Cdd:COG1566 88 AEAQLAAAEAQL-ARLEAELGAEAEIAAAEAQ-LAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDAAQAQLE 165
|
90 100
....*....|....*....|....*.
gi 31982223 1769 GKAAQLDGLEARMRSVLQAINLQVQI 1794
Cdd:COG1566 166 AAQAQLAQAQAGLREEEELAAAQAQV 191
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1551-1789 |
2.11e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 44.97 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIAERVRSLADVDTILAHTMGDV-RRAEQLLQDAHRArsraegeRQKAETVQAALEEAQRAqgAAQGAIwga 1629
Cdd:smart00283 7 EEIAAGAEEQAEELEELAERMEELSASIEEVaANADEIAATAQSA-------AEAAEEGREAVEDAITA--MDQIRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1630 vvDTQNTEQTLQRVQERMAGAEKSLNSAGERARQ-----LDALLEAlklKRAGNS------LAA---STAEETAGSA--- 1692
Cdd:smart00283 75 --VVEEAVSAVEELEESSDEIGEIVSVIDDIADQtnllaLNAAIEA---ARAGEAgrgfavVADevrKLAERSAESAkei 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1693 QSRAREAEKQLREQVGDQYQTVR------ALAERK-------AEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGT 1759
Cdd:smart00283 150 ESLIKEIQEETNEAVAAMEESSSeveegvELVEETgdaleeiVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQV 229
|
250 260 270
....*....|....*....|....*....|
gi 31982223 1760 YEENERALEGKAAQLDGLEARMRSVLQAIN 1789
Cdd:smart00283 230 TQETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1452-1707 |
2.18e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 45.11 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1452 LALGRARHTQAELQRALvegggilsRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvkdflsqegADP 1531
Cdd:COG2956 46 LALGNLYRRRGEYDRAI--------RIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE----------LDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1532 DSIEmVATRVLDISipaspEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQ 1609
Cdd:COG2956 108 DDAE-ALRLLAEIY-----EQEGDWekAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1610 AALEEAQRAQGAAQGAIwgavvdtqnteQTLQRVQERMAGAEKSLNSAGERARQLDALLEALK-LKRAGNSLAASTAEET 1688
Cdd:COG2956 182 LLLAELYLEQGDYEEAI-----------AALERALEQDPDYLPALPRLAELYEKLGDPEEALElLRKALELDPSDDLLLA 250
|
250 260
....*....|....*....|..
gi 31982223 1689 AGS---AQSRAREAEKQLREQV 1707
Cdd:COG2956 251 LADlleRKEGLEAALALLERQL 272
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1443-1781 |
2.35e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1443 CSGAAATADLALGRARHTQAELQRALVEGGGIL-------------------SRVSETRRQAEEAQQRAQAAL----DKA 1499
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLrlapDKL 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1500 NASRGQVEQANQELRELI------QNVKDFLSQEgadpdsiemvatrvldisIPASPEQIQRLASEIAERVRSLADVDTI 1573
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLglapgrQSIIDLKEKE------------------IPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1574 LAHTMGDVRRAEQLLQDAhrarsraegerQKAETVQAALEEAQR--AQGAA--QGAIWGAVV-----DTQNTEQTLQRVQ 1644
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDV-----------TIMERFQMELKDVERkiAQQAAklQGSDLDRTVqqvnqEKQEKQHELDTVV 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1645 ERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE------KQLREQVGDQYQTVRALA 1718
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQslireiKDAKEQDSPLETFLEKDQ 922
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982223 1719 ERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEEN-ERALEGKAAQLDGLEARM 1781
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQL 986
|
|
| DUF4398 |
pfam14346 |
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. ... |
1444-1509 |
3.22e-04 |
|
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 127 and 269 amino acids in length.
Pssm-ID: 464144 [Multi-domain] Cd Length: 78 Bit Score: 41.09 E-value: 3.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1444 SGAAATADLALGRARHTQAELQRALVEGggilsRVSETRRQAEEAQQRAQAALDKANA--SRGQVEQA 1509
Cdd:pfam14346 16 DGAAQYAPLELKRARDALAKAEAAMAEK-----DYEKARHLAYLAEADAELAEAKARAakAEAAAAQA 78
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1482-1766 |
3.32e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1482 RRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflsQEgadpdsiemvatRVLDisipaspEQIQRLASEIA 1561
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EE------------REED-------ERILEYLKEKA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1562 ERVRSladvdtilahtmgdvRRAEQLLQDA----HRARSRAEGERQKAEtvQAALEE--AQRAQgAAQGAIWgavvdtqn 1635
Cdd:pfam13868 166 EREEE---------------REAEREEIEEekerEIARLRAQQEKAQDE--KAERDElrAKLYQ-EEQERKE-------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1636 teqtlqRVQERMAgAEKslnsageRARQLDALLealklkragnslaastaeetagsaqsRAREAEKQLREQvgdQYQTVR 1715
Cdd:pfam13868 220 ------RQKEREE-AEK-------KARQRQELQ--------------------------QAREEQIELKER---RLAEEA 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 31982223 1716 ALAERKAEGVLAAQARaeqlrDEARDLLQAAQDKLQRLQ---ELEGTYEENERA 1766
Cdd:pfam13868 257 EREEEEFERMLRKQAE-----DEEIEQEEAEKRRMKRLEhrrELEKQIEEREEQ 305
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1582-1749 |
3.47e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.36 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1582 RRAEQLLQDAHRARSRAEGERQKAE--TVQAALE-------EAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEK 1652
Cdd:PRK07735 16 RRAKEEARKRLVAKHGAEISKLEEEnrEKEKALPknddmtiEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1653 SlnsAGERARQLDAllEALKLKRAGNSLA-----ASTAEETAGSAQSRAREAEKQLRE--QVGDQYQTVRALAERKAEGV 1725
Cdd:PRK07735 96 K---AAAAAKAKAA--ALAKQKREGTEEVteeekAAAKAKAAAAAKAKAAALAKQKREgtEEVTEEEEETDKEKAKAKAA 170
|
170 180
....*....|....*....|....*...
gi 31982223 1726 LAAQARA----EQLRDEARDLLQAAQDK 1749
Cdd:PRK07735 171 AAAKAKAaalaKQKAAEAGEGTEEVTEE 198
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1789 |
3.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1694 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARDL-LQAAQDKL----QRLQELEGTYEENERALE 1768
Cdd:COG4913 238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312
|
90 100
....*....|....*....|.
gi 31982223 1769 GKAAQLDGLEARMRSVLQAIN 1789
Cdd:COG4913 313 RLEARLDALREELDELEAQIR 333
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1453-1671 |
3.72e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1453 ALGRARHTQ----AELQRALVEGGGILsRVSETRRQAEEAQQRAQAALDKAnasrgQVEQANQELRELIQNVKdfLSQEG 1528
Cdd:COG2268 188 ALGRRKIAEiirdARIAEAEAERETEI-AIAQANREAEEAELEQEREIETA-----RIAEAEAELAKKKAEER--REAET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1529 AdpdsiEMVATRVLDISIPASPEQIQRLAsEIAERVRSLAdvdtiLAHtmgdvRRAEQLLQDAHRA-RSRAEGERQKAET 1607
Cdd:COG2268 260 A-----RAEAEAAYEIAEANAEREVQRQL-EIAEREREIE-----LQE-----KEAEREEAELEADvRKPAEAEKQAAEA 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982223 1608 VQAALEEAQRAQGAAQGAiwgavvdtqnteqtlqrVQERMAGAEKSLNSAGErarqLDALLEAL 1671
Cdd:COG2268 324 EAEAEAEAIRAKGLAEAE-----------------GKRALAEAWNKLGDAAI----LLMLIEKL 366
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
1603-1738 |
3.86e-04 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 41.88 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1603 QKAETvqaALEEAQRAQGAAQGAIwgavvdtQNTEQTLQRVQERMAGAEKSLNSAGERARQ--LDALLEALKLKRagNSL 1680
Cdd:pfam02050 1 DEAAR---ELAEAQRELQQAEEKL-------EELQQYRAEYQQQLSGAGQGISAAELRNYQafISQLDEAIAQQQ--QEL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1681 AASTAEetagsaQSRAREA--EKQLReqvgdqYQTVRALAERKAEGVLAAQARAEQLR-DE 1738
Cdd:pfam02050 69 AQAEAQ------VEKAREEwqEARQE------RKSLEKLREREKKEERKEQNRREQKQlDE 117
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1603-1768 |
3.92e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 45.05 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1603 QKAETV-QAALEEAQRAQG-AAQGAIWgavvdTQNTEQTLQRVQERMAGAEKSLNsageRARQLDALLEALKLKRAgnsl 1680
Cdd:pfam15070 1 QLMESLkQLQTERDQYAENlKEEGAVW-----QQKMQQLSEQVRTLREEKERSVS----QVQELETSLAELKNQAA---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1681 AASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAerkaegvlaAQARAeQLRD-EARDLLQAAQDklQRLQELEGT 1759
Cdd:pfam15070 68 VPPAEEEQPPAGPS---EEEQRLQEEAEQLQKELEALA---------GQLQA-QVQDnEQLSRLNQEQE--QRLLELERA 132
|
170
....*....|....*.
gi 31982223 1760 YE-------ENERALE 1768
Cdd:pfam15070 133 AErwgeqaeDRKQILE 148
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1718-1794 |
4.03e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 42.30 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1718 AERKAEGVLAAQARAEQL----RDEARDLLQAAQDKLQRL-QELEG-TYEENERALEGKAAQLDGLEARMRSVL--QAIN 1789
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121
|
....*
gi 31982223 1790 LQVQI 1794
Cdd:pfam00430 122 LAVQI 126
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
1578-1752 |
4.21e-04 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 45.29 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1578 MGDVRRAEQLLQDAHRARSRAEGERQKAeTVQAA--LEEAQRAQGAAQGAiwgavVDTQntEQTLQRVQERMAG------ 1649
Cdd:NF040586 533 LGDYREALELDREVLRRRRRVLGPDHPR-TLLSAnnLARDLRELGRYAEA-----LDLL--EEALERYREVLGGpdhpdt 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1650 --AEKSLNSAgerARQLDALLEALKLKR-------------------AGNSLAA--STAEETAGsAQSRAREAEKQLREQ 1706
Cdd:NF040586 605 lrAAKSLAVA---LRRAGRLEEALELAEdtyeryrrrfgpdhpdtlaAALSLANdlRALGDADE-ARELAREVLDRYRRV 680
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31982223 1707 VGDQYQTVRAlaerkAEGVLAAQARAEQLRDEARDLLQAAQDKLQR 1752
Cdd:NF040586 681 LGEDHPFTLA-----CRNNLAVLLRALGDPEEARELAEAALEGLRE 721
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
1529-1772 |
4.56e-04 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 44.97 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1529 ADPDSIEMVA-TRVLDISI-------------PASPEQiqRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAHRA 1594
Cdd:pfam04632 118 ADPEAIFDIAvARVSEISLgilcaalvsalvfPRSVGP--ALRARLRARLRDAL-------------RLAAAALAGAPGA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1595 RSRAEGERQKAETVqAALEeAQRAQGAAQGAiwgavvdtqnteqtlqRVQERMAGAeKSLNsagerARQLDALLEALKLK 1674
Cdd:pfam04632 183 EAFEAARLRLAADI-LALE-ALRSHAAFESP----------------RGRARARAL-RRLL-----ARMLALLPRLRSLA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1675 RAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQLRDEARDLLQAAQDKLQRLQ 1754
Cdd:pfam04632 239 RLLARLRTEGAGTVPELAALLDELAAWEAALAAEALQAALAALRAR----LRALRPALPLDFDTAAELLARLADLLAELA 314
|
250
....*....|....*...
gi 31982223 1755 ELEGTYEENERALEGKAA 1772
Cdd:pfam04632 315 EALASCRALRHPIAQGAR 332
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
878-917 |
4.75e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 4.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 31982223 878 CVCNGR---ADECDTHTGACLgCRDYTGGEHCERCIAGFHGDP 917
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| HemYx |
COG3071 |
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
1445-1746 |
4.80e-04 |
|
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];
Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 44.52 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1445 GAAATAD--LALGRARHTQAE--LQRAlvegggilsrvsetrrqAEEAQQRAQAALDKANAS--RGQVEQANQELRELIQ 1518
Cdd:COG3071 16 LLAALLEglLALAEGRYARAEklLSKA-----------------AEHSEAPLLAYLLAARAAqaLGDYERRDEYLAQALE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1519 NvkdflsqegaDPDSIEMVATRVLDISI-----PASPEQIQRLASEIAERVRSLAdvdtILAHTMGDVRRAEQLLQ---- 1589
Cdd:COG3071 79 L----------APEAELAVLLTRAELLLdqgqaEQALATLEALRAGAPRHPQVLR----LLLQAYRQLGDWEELLEllpa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1590 -DAHRARSRAEGERQKAETVQAALEEAqrAQGAAQ-GAIWGAVVDTqntEQTLQRVQERMAGAEKSLNsAGERARQLdaL 1667
Cdd:COG3071 145 lRKHKALSAEEAQALERRAYLGLLRQA--ARDAEAlKALWKALPRA---ERRDPELAAAYARALIALG-DHDEAERL--L 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982223 1668 LEALKlKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQyqtvrALAErkaegVLAAQARAEQLRDEARDLLQAA 1746
Cdd:COG3071 217 REALK-RQWDPRLVRLYGRLQGGDPAKQLKRAEKWLKKHPNDP-----DLLL-----ALGRLCLRNQLWGKAREYLEAA 284
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1551-1672 |
5.63e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 41.42 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRL---ASEIAERVRSLADVDTilahtmgDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRaqgaaqgaiw 1627
Cdd:pfam18595 9 EELAELerkARELQAKIDALQVVEK-------DLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEI---------- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31982223 1628 gAVVDTQNTEQTLQR----VQERMAGAEKslnSAGERARQLDALLEALK 1672
Cdd:pfam18595 72 -ELRELERREERLQRqlenAQEKLERLRE---QAEEKREAAQARLEELR 116
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1554-1630 |
6.00e-04 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.88 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1554 QRLASEIAERVRSLAD-VDTILAHTMGDVRRAE--------------QLLQDAHRARSRAEGERQKAETVQAALEEAQRA 1618
Cdd:pfam16999 4 SRLLSELAEREAALDQqIEAARKEAEREVEAAEaeaarilreaeakaKALQAEYRQELAAETARIREEARARAEAEAQAV 83
|
90
....*....|..
gi 31982223 1619 QGAAQGAIWGAV 1630
Cdd:pfam16999 84 RTRAEGRLQQAV 95
|
|
| outer_NodT |
TIGR01845 |
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this ... |
1444-1793 |
6.06e-04 |
|
efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family; Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins]
Pssm-ID: 273830 [Multi-domain] Cd Length: 460 Bit Score: 44.32 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1444 SGAAATADLALGRARHTQAELQRALvegggilsrvSETRRQAEEAQQRAQAALDKAN---ASRGQVEQANQELRELIQNV 1520
Cdd:TIGR01845 168 SASIANAYVQLAALRAQLDVYHAAL----------ASRRKTLELTQKRYAAGVAAASdvrQAEAAVASAEAELPSLDVQI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1521 KdfLSQE------GADPDsiemvatRVLDISIPASPEQIQ-RLASEI-AERVRSLADVdtilahtmgdvrraeqllqdah 1592
Cdd:TIGR01845 238 A--QARNalaallGKGPS-------RGLAIARPLLLDQLPpDLPLSLpSDLLRRRPDI---------------------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1593 rarsrAEGERQkaetvqaaLEEAQRAQGAAQGAIWGAVvdtqnteqTLQrvqermagaekslNSAGERARQLDALLEALK 1672
Cdd:TIGR01845 287 -----RAAERR--------LAAANAQIGVAKAAFFPSI--------TLS-------------ASIGLSASQLSRLFDGGS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1673 LKRA-GNSLAASTAEetAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDeARDLLQAAQDKLQ 1751
Cdd:TIGR01845 333 RFWSiGPALALPIFD--GGSLRAALDSAKATYDAAVAQYRQTVLTAFQEVADALVALQALARRLDA-QRQAVEQAQEALS 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 31982223 1752 RLQelegtyeENERAleGKAAQLDGLEARmRSVLQA----INLQVQ 1793
Cdd:TIGR01845 410 LAQ-------TRYRA--GLDSYLTVLEAQ-RSLLTAqrslATLQAR 445
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1582-1623 |
7.19e-04 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 39.67 E-value: 7.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 31982223 1582 RRAEQLLQDAHRARSRAEGERQKA----ETVQAALEEAQRAQGAAQ 1623
Cdd:pfam11839 8 SKADQAEQDAAAAQSAADSAKAKAdeaaARANAAEAAAEEAQQAAE 53
|
|
| HrpE_YscL_not |
TIGR02499 |
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ... |
1561-1690 |
8.55e-04 |
|
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274165 [Multi-domain] Cd Length: 166 Bit Score: 41.90 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1561 AERVRSLADVDTILAHTmgdVRRAEQLLQDAHRarsraEGERQKAETVQAALEEAQRAQgAAQGAIWgavvdTQNTEQTL 1640
Cdd:TIGR02499 6 AEDLAALAQAQAILAAA---RQRAEAILADAEE-----EAEASRQLGYEQGLEQFWQEA-AAQLAEW-----QQEAEQLE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 31982223 1641 QRVQERMAGAeksLNSAGERArqLDALLEALKLKRAGNSLAASTAEETAG 1690
Cdd:TIGR02499 72 ASLEERLAEL---VLQALEQI--LGEYDEPERLVRLLRQLLRAVANQGRL 116
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1587-1782 |
8.66e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.17 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1587 LLQDAHRarSRAEGERQKAETVqaaLEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDA 1666
Cdd:pfam06008 33 SPENAHK--IQIEILEKELSSL---AQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1667 LLEalklkragnslaasTAEETAGSAQSRA-REAEKQLREQVGDQYQTVRALAErkaegvlaaqaraEQLrDEARDLLQA 1745
Cdd:pfam06008 108 LGE--------------NDFALPSSDLSRMlAEAQRMLGEIRSRDFGTQLQNAE-------------AEL-KAAQDLLSR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 31982223 1746 AQDKLQRLQ-ELEGTYEENERALEGKAAQLDGLEARMR 1782
Cdd:pfam06008 160 IQTWFQSPQeENKALANALRDSLAEYEAKLSDLRELLR 197
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1512-1780 |
8.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1512 ELRELIQNVKDFLSQEgadpdsiemvatrvldisipaspEQIQRLASEIAERvrsladvdtiLAHTMGDVRRAEQLLQDA 1591
Cdd:PRK03918 173 EIKRRIERLEKFIKRT-----------------------ENIEELIKEKEKE----------LEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1592 HRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGavvdtqnTEQTLQRVQERMAGAEKSLNSAGERARQLDAL---- 1667
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-------LEEKIRELEERIEELKKEIEELEEKVKELKELkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1668 LEALKLKRAGNSL--AASTAEETAGSAQSRAREAEKQLREqvgdqyqtvralAERKAEgvlaaqaRAEQLRDEARDLLQa 1745
Cdd:PRK03918 293 EEYIKLSEFYEEYldELREIEKRLSRLEEEINGIEERIKE------------LEEKEE-------RLEELKKKLKELEK- 352
|
250 260 270
....*....|....*....|....*....|....*
gi 31982223 1746 aqdklqRLQELEGTYEENERALEgKAAQLDGLEAR 1780
Cdd:PRK03918 353 ------RLEELEERHELYEEAKA-KKEELERLKKR 380
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1654-1783 |
8.82e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1654 LNSAGERA----RQLD-ALLEALK-LKRAGNSLAASTAEETagSAQSRAREAEKQLRE---------QVGDQyQTVRALA 1718
Cdd:COG1842 14 INALLDKAedpeKMLDqAIRDMEEdLVEARQALAQVIANQK--RLERQLEELEAEAEKweekarlalEKGRE-DLAREAL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982223 1719 ERKAEgvlaAQARAEQLRdEARDLLQAAQDKLQR-LQELEGTYEENEralegkaAQLDGLEARMRS 1783
Cdd:COG1842 91 ERKAE----LEAQAEALE-AQLAQLEEQVEKLKEaLRQLESKLEELK-------AKKDTLKARAKA 144
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1604-1793 |
9.84e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1604 KAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGER----ARQLDALLEALKLKRAGNS 1679
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkeeLRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1680 -LAASTAEETagSAQSRAREAEKQ-LREQVGDqyqtVRALAERKAEgvlaAQARAEQLRDEARDLLQaaqdklQRLQEle 1757
Cdd:pfam07888 108 aSSEELSEEK--DALLAQRAAHEArIRELEED----IKTLTQRVLE----RETELERMKERAKKAGA------QRKEE-- 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 31982223 1758 gtyEENERALEGKAAQLDGLEARMRSVLQ-AINLQVQ 1793
Cdd:pfam07888 170 ---EAERKQLQAKLQQTEEELRSLSKEFQeLRNSLAQ 203
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
1548-1792 |
1.01e-03 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 43.51 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1548 ASPEQI-QRLASEIAERVRSLADVDTI-LAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAAleeAQRAQGAAQGA 1625
Cdd:PRK01294 102 LDLAAIdALVEREIAAQLPEPADSQALdLWLRYKAYLSALAQLEDDGPGKLDLQALQQLLDARLAL---RARFFSDWEIQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1626 IWGAvvdtqnTEQTLQRVQ-ERMAGAEKSLNSAGERARQLDALLEALKlkragnslAASTAEETAGSAQSRAREAEKQLR 1704
Cdd:PRK01294 179 AFFG------EENQYQRYAlERLRIAQDPSLSDAQKAARLAALEAQLP--------EDLRAALQESQRQQALLQQLAQLQ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1705 EQVGDQYQTVRALAErkAEGVLAAQaRAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERAlegKAAQLDGLEARMRSV 1784
Cdd:PRK01294 245 ASGASPQELRLMRAQ--LVGPEAAQ-RLEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQD---RQAQIAQLRQQRFSP 318
|
....*...
gi 31982223 1785 LQAINLQV 1792
Cdd:PRK01294 319 QEALRLAA 326
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1487-1778 |
1.02e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1487 EAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRS 1566
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1567 LADVDTILahtmgdVRRAEQLLQDAHRARSRAEGERQKA--ETVQAALEEAQRAQGAAQGAIWGAVVDT-QNTEQTLQRV 1643
Cdd:COG5185 352 LTENLEAI------KEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEEL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1644 QERMAGAEKSLNsagERARQLDALLEAL-KLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKA 1722
Cdd:COG5185 426 QRQIEQATSSNE---EVSKLLNELISELnKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 1723 EGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENE-RALEGKAAQLDGLE 1778
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLiPASELIQASNAKTD 559
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1583-1757 |
1.03e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1583 RAEQLLQD------AHRaRSRAEGERQKAETVQAALEEAQRaqgaaqgaiwgavvdTQNTEQTLQRVQERMAGAEKSLNS 1656
Cdd:pfam05557 10 RLSQLQNEkkqmelEHK-RARIELEKKASALKRQLDRESDR---------------NQELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1657 AGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRARE-------AEKQLREQVGDQYQTVRALAERKAEgvlaaQ 1729
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSElrrqiqrAELELQSTNSELEELQERLDLLKAK-----A 148
|
170 180 190
....*....|....*....|....*....|..
gi 31982223 1730 ARAEQLRDEardlLQAAQDKL----QRLQELE 1757
Cdd:pfam05557 149 SEAEQLRQN----LEKQQSSLaeaeQRIKELE 176
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1645-1752 |
1.14e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1645 ERMAGAEKSLNSAgERAR-QLDALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVgdqyqtvRALAERKAE 1723
Cdd:COG0711 31 ERQEKIADGLAEA-ERAKeEAEAALAEYEEKLAE---ARAEAAEIIAEARKEAEAIAEEAKAEA-------EAEAERIIA 99
|
90 100 110
....*....|....*....|....*....|....*...
gi 31982223 1724 gvlAAQARAEQ--------LRDEARDL-LQAAQDKLQR 1752
Cdd:COG0711 100 ---QAEAEIEQerakalaeLRAEVADLaVAIAEKILGK 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1203-1462 |
1.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1203 QDLAARTRRLEQWAQELQQTG--------VLGAfeSSFLNMQGKLGMVQAIMSARNASAASTAKLVEATEGLRHEIGKTT 1274
Cdd:COG3883 79 AEIEERREELGERARALYRSGgsvsyldvLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1275 ERLTQLEAELTAVQDEnfnANHALSglERDGLALNLTLRQLDQHLEILKHSNFLGAYDSIRHAHSQSTEAERRANASTFA 1354
Cdd:COG3883 157 AELEALKAELEAAKAE---LEAQQA--EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1355 VPSPVSNSADTRRrtevlMGAQKENFNRQHLANQQALGRLSAHAHTLSLTGINELVCGAPGDAPCATSPCGGAGCRDEDG 1434
Cdd:COG3883 232 AAAAAAAAAAAAA-----SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGG 306
|
250 260
....*....|....*....|....*...
gi 31982223 1435 QPRCGGLGCSGAAATADLALGRARHTQA 1462
Cdd:COG3883 307 SGGAGGVGSGGGAGAVVGGASAGGGGGS 334
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1634-1735 |
1.30e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 40.76 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1634 QNTEQTLQRVQERMAGAEKSLNSAgeRARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQt 1713
Cdd:pfam00430 33 ELIADEIAEAEERRKDAAAALAEA--EQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKD- 109
|
90 100
....*....|....*....|..
gi 31982223 1714 vRALAERKAEGVLAAQARAEQL 1735
Cdd:pfam00430 110 -RALAELRQQVVALAVQIAEKL 130
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1445-1755 |
1.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1445 GAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELI------- 1517
Cdd:PRK04863 957 QAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA---QLAQYNQVLASLKssydakr 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1518 QNVKDFlsqegadpdsiemvATRVLDISIPASPEQIQRLAS---EIAERVRSladvdtilahtmGDVRRAEqllqdAHRA 1594
Cdd:PRK04863 1034 QMLQEL--------------KQELQDLGVPADSGAEERARArrdELHARLSA------------NRSRRNQ-----LEKQ 1082
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1595 RSRAEGERQKAETVQAALEE---AQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAgAEKSLNSAGERarqLDALLEAL 1671
Cdd:PRK04863 1083 LTFCEAEMDNLTKKLRKLERdyhEMREQVVNAKAGWCAVLRLVKDNGVERRLHRREL-AYLSADELRSM---SDKALGAL 1158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1672 KLKRAGN-----SLAAStaeETagsaqSRAREAEKQLreqvgdqYQTVRALaerkaegvLAAQARAEQLR-DEARDLLQA 1745
Cdd:PRK04863 1159 RLAVADNehlrdVLRLS---ED-----PKRPERKVQF-------YIAVYQH--------LRERIRQDIIRtDDPVEAIEQ 1215
|
330
....*....|
gi 31982223 1746 AQDKLQRLQE 1755
Cdd:PRK04863 1216 MEIELSRLTE 1225
|
|
| DUF1631 |
pfam07793 |
Protein of unknown function (DUF1631); The members of this family are sequences derived from a ... |
1474-1664 |
1.94e-03 |
|
Protein of unknown function (DUF1631); The members of this family are sequences derived from a group of hypothetical proteins expressed by certain bacterial species. The region concerned is approximately 440 amino acid residues in length.
Pssm-ID: 429661 Cd Length: 742 Bit Score: 43.08 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1474 ILSRVSETRRQAEEAQQRAQAAL---DKANASRGQVEqanQELRELIQN------VKDFLSQ------------EGAD-P 1531
Cdd:pfam07793 459 FEEFLERERRRAELAEQRTVDAAegrERLELARQQAA---DELEQRLAGrplpevVREFLRQawsdvlaltylrHGEDsE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1532 DSIEMVAT------RVLDISIPASPEQIQRLASEIAERVRS-LADVdtilAHTMGDVRRAEQLLQDAHRARSRAEGERQK 1604
Cdd:pfam07793 536 EWQEALATaddlvwSVSPKPTAEERARLLALLPELLKRLRQgLASI----GYDPDESEAFFKELEALHAAAFRAKAAALA 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1605 AETVQAALEEAQRAQGAaqgaiwgAVVDTQNTEQTLQRVQERMAGAEKSLNSAG-ERARQL 1664
Cdd:pfam07793 612 AALKAAAAKPAPAAAPA-------SPVEAEEEEALLGADAPPLAVVASPEDDAYlAQARAL 665
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1476-1789 |
1.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1476 SRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQ-IQ 1554
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKrLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1555 RLASEIAERVRSLADVDTilahtmgDVRRAEQL---LQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGaiwgavV 1631
Cdd:PRK03918 318 RLEEEINGIEERIKELEE-------KEERLEELkkkLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG------L 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1632 DTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALK-----LKRA----------------GNSLAASTAE-ETA 1689
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaieeLKKAkgkcpvcgrelteehrKELLEEYTAElKRI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1690 GSAQSRAREAEKQLREQvgdqyqtvralaERKAEGVLAAQARAEQLRDEArDLLQAAQDKLQR--LQELEGTYEENERAL 1767
Cdd:PRK03918 465 EKELKEIEEKERKLRKE------------LRELEKVLKKESELIKLKELA-EQLKELEEKLKKynLEELEKKAEEYEKLK 531
|
330 340
....*....|....*....|..
gi 31982223 1768 EgkaaQLDGLEARMRSVLQAIN 1789
Cdd:PRK03918 532 E----KLIKLKGEIKSLKKELE 549
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
1659-1790 |
2.08e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 40.43 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1659 ERARQLDALLEALKLKRA------GNSLAASTAEETAGSAQsrAREAEKQLReqvgdqyQTVRALAERKAEGVLAAQARA 1732
Cdd:pfam05130 9 EELELLEELLELLEEEQEalkagdIEALEELTEEKQELLQK--LAQLEKERR-------ELLAELGLSPEEATLSELLAK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982223 1733 EQLRDEARDLLQAAQDKLQRLQELEgtyEENERAlegkaaqldgLEARMRSVLQAINL 1790
Cdd:pfam05130 80 EEEDPELRELWQELLELLERLKELN---ELNGEL----------IEQSLEFNNRSLNI 124
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1467-1674 |
2.39e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1467 ALVEGGGILSRVSETRRQAEEAQqrAQAALDKAnasRGQVEQANQELRELiQNVKDFLSQEGADPDSIEmVATRVLDISI 1546
Cdd:pfam00529 40 DRVKAGDVLFQLDPTDYQAALDS--AEAQLAKA---QAQVARLQAELDRL-QALESELAISRQDYDGAT-AQLRAAQAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1547 PASPEQIQrLASEIAERVRSLADVDTILAHTMGDVRRAeqllqdahrarsraegerqkAETVQAALEEAQRAQGAAQGAI 1626
Cdd:pfam00529 113 KAAQAQLA-QAQIDLARRRVLAPIGGISRESLVTAGAL--------------------VAQAQANLLATVAQLDQIYVQI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 31982223 1627 wgavvdTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLK 1674
Cdd:pfam00529 172 ------TQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1637-1782 |
2.71e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 41.19 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1637 EQTLQRVQ---ERMAGAEKSLNSA----GERARQLDALLE--ALKLKRAGNSLAaSTAEETAGSAQSRAREAEKQLREQV 1707
Cdd:cd07596 17 EEQLKKLSkqaQRLVKRRRELGSAlgefGKALIKLAKCEEevGGELGEALSKLG-KAAEELSSLSEAQANQELVKLLEPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1708 GDQYQTVRA----LAERKAEG--VLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARM 1781
Cdd:cd07596 96 KEYLRYCQAvketLDDRADALltLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERL 175
|
.
gi 31982223 1782 R 1782
Cdd:cd07596 176 K 176
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1580-1755 |
2.73e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 41.95 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1580 DVRRAEQLLQDAHRARSRAEGER----------QKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAG 1649
Cdd:COG1538 15 DLRAARARVEAARAQLRQARAGLlpsqeldlggKRRARIEAAKAQAEAAEADLRAARLDLAAEVAQAYFDLLAAQEQLAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1650 AEKSLNSAGERARQLDALLEA-----LKLKRAGNSLAASTAEETAgsAQSRAREAEKQLREQVGDQYQTVRALAERKAEG 1724
Cdd:COG1538 95 AEENLALAEELLELARARYEAglasrLDVLQAEAQLAQARAQLAQ--AEAQLAQARNALALLLGLPPPAPLDLPDPLPPL 172
|
170 180 190
....*....|....*....|....*....|...
gi 31982223 1725 VLAAQARAEQLRD--EARDLLQAAQDKLQRLQE 1755
Cdd:COG1538 173 PPLPPSLPGLPSEalERRPDLRAAEAQLEAAEA 205
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1510-1755 |
2.82e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.28 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1510 NQELREL---IQNVKDFLSQE--GADPDSIEmvatrvldisipASPEQIQRLASEIAERVRSLADVDtilahtmgdvRRA 1584
Cdd:cd00176 6 LRDADELeawLSEKEELLSSTdyGDDLESVE------------ALLKKHEALEAELAAHEERVEALN----------ELG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1585 EQLLQDAHRArsraegerqkAETVQAALEEAQRAqgaaqgaiWgavvdtqnteqtlQRVQERMAGAEKSLNSAGERARQL 1664
Cdd:cd00176 64 EQLIEEGHPD----------AEEIQERLEELNQR--------W-------------EELRELAEERRQRLEEALDLQQFF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1665 DALLEALK-LKRAGNSLAASTAEETAGSAQSRAREaEKQLREQVgDQYQTVRALAERKAEGVLAA---------QARAEQ 1734
Cdd:cd00176 113 RDADDLEQwLEEKEAALASEDLGKDLESVEELLKK-HKELEEEL-EAHEPRLKSLNELAEELLEEghpdadeeiEEKLEE 190
|
250 260
....*....|....*....|.
gi 31982223 1735 LRDEARDLLQAAQDKLQRLQE 1755
Cdd:cd00176 191 LNERWEELLELAEERQKKLEE 211
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1454-1542 |
2.94e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 40.29 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1454 LGRA-RHTQAELQRALVEGGGILSRVSEtRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSqegadpD 1532
Cdd:PRK14473 58 LANAkRDYEAELAKARQEAAKIVAQAQE-RARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIA------D 130
|
90
....*....|
gi 31982223 1533 SIEMVATRVL 1542
Cdd:PRK14473 131 LVTLTASRVL 140
|
|
| Ala_zip_lipo |
NF040598 |
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ... |
1583-1618 |
2.98e-03 |
|
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.
Pssm-ID: 468572 [Multi-domain] Cd Length: 90 Bit Score: 38.43 E-value: 2.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 31982223 1583 RAEQLLQDAHRARSRAEGERQKAE----TVQAALEEAQRA 1618
Cdd:NF040598 37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1551-1671 |
3.10e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.16 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1551 EQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAH------RARSRAEGERQKAETVQAALEEAQRAQGAAQG 1624
Cdd:COG0711 31 ERQEKIADGLAEAERAKEEAEAALA-------EYEEKLAEARaeaaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEA 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 31982223 1625 AIwgavvdTQNTEQTLQRVQER-----MAGAEKSLN---SAGERARQLDALLEAL 1671
Cdd:COG0711 104 EI------EQERAKALAELRAEvadlaVAIAEKILGkelDAAAQAALVDRFIAEL 152
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
309-341 |
3.39e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.33 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|...
gi 31982223 309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
350-403 |
3.76e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 31982223 350 CECNG---HTHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCEFCRPFFYRDPTKD 403
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1579-1769 |
4.39e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1579 GDVRRAEQLLQDAHRARSRAEGERQKAEtvQAALEEAQRAQGAAQGAIwgavvdtqnteqtlqRVQErmAGAEKSLNSAG 1658
Cdd:COG2268 223 AEEAELEQEREIETARIAEAEAELAKKK--AEERREAETARAEAEAAY---------------EIAE--ANAEREVQRQL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1659 ERARQldalLEALKLKRAgnslaastaeetagSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLA---AQARAEQL 1735
Cdd:COG2268 284 EIAER----EREIELQEK--------------EAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAkglAEAEGKRA 345
|
170 180 190
....*....|....*....|....*....|....
gi 31982223 1736 RDEARDLLQAAQDKLQRLQELEGTYEENERALEG 1769
Cdd:COG2268 346 LAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEK 379
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1581-1773 |
4.70e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1581 VRRAEQLLQDAHRARSRAEG-----ERQKAE------------------TVQAALEEAQRAQ-GAAQGAIWGAVVDTQNT 1636
Cdd:PRK05035 438 IRAIEQEKKKAEEAKARFEArqarlEREKAArearhkkaaearaakdkdAVAAALARVKAKKaAATQPIVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1637 EQTLQRVQERMAGAEK-----SLNSAGERARQLDALLEALKLKRAGNSLAASTAEE---------TAGSAQSRAREAEKQ 1702
Cdd:PRK05035 518 AVIAAREARKAQARARqaekqAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEevdpkkaavAAAIARAKAKKAAQQ 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982223 1703 LREQvgDQYQTVRALAERKAEgVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGtyeENERALEGKAAQ 1773
Cdd:PRK05035 598 AASA--EPEEQVAEVDPKKAA-VAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAA---AIARAKARKAAQ 662
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1692-1790 |
5.37e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1692 AQSRAREAEKQLREQVGDQyqtvRALAERKAegvlaaqaRAEQLRDEARDLLQAAQDKLQRLQELEGTYEE--------- 1762
Cdd:pfam13851 66 AQEEVEELRKQLENYEKDK----QSLKNLKA--------RLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfeaai 133
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 31982223 1763 ----------N---ERALEGKAAQLDGLEARMRSVLQAINL 1790
Cdd:pfam13851 134 qdvqqktglkNlllEKKLQALGETLEKKEAQLNEVLAAANL 174
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1604-1776 |
6.08e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.43 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1604 KAETVqAALEEAQRAQGAAQGAIWGAVVDTQnTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAAS 1683
Cdd:PRK12678 48 KGELI-AAIKEARGGGAAAAAATPAAPAAAA-RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1684 TAEETAGSAQSRAREAEKQLREQVGDQyqtvrALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEEN 1763
Cdd:PRK12678 126 QARERRERGEAARRGAARKAGEGGEQP-----ATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG 200
|
170
....*....|...
gi 31982223 1764 ERALEGKAAQLDG 1776
Cdd:PRK12678 201 DDRDRRDRREQGD 213
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1474-1632 |
6.34e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1474 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRvldisipaspEQI 1553
Cdd:cd22656 119 IKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEIKDLQ----------KEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1554 QRLASEIAERVR-SLADVDTILAHTMGDVRRAEQLLQDAHRArsraegeRQKAETVQAALEEAQRAQGAAQGAiWGAVVD 1632
Cdd:cd22656 189 EKLNEEYAAKLKaKIDELKALIADDEAKLAAALRLIADLTAA-------DTDLDNLLALIGPAIPALEKLQGA-WQAIAT 260
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1462-1614 |
7.57e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1462 AELQRALVEG-GGILSRVSETRRQAEEAQQ---RAQAALDKANASRGQVEQANQELRELIQNVkDFlsqegaDPDSIEMV 1537
Cdd:COG0497 229 QEALEALSGGeGGALDLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSL-EF------DPERLEEV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1538 ATRVLDISIPA-----SPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDA----HRARSRAegerqkAETV 1608
Cdd:COG0497 302 EERLALLRRLArkygvTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAaeklSAARKKA------AKKL 375
|
....*.
gi 31982223 1609 QAALEE 1614
Cdd:COG0497 376 EKAVTA 381
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
1662-1755 |
7.99e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 38.30 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1662 RQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREaekqlreqvgdqyqtVRALAERKAEGVLA-AQARAEQLRDEAR 1740
Cdd:COG3599 44 KELKEKLEELEEELEEYRELEETLQKTLVVAQETAEE---------------VKENAEKEAELIIKeAELEAEKIIEEAQ 108
|
90
....*....|....*
gi 31982223 1741 DLLQAAQDKLQRLQE 1755
Cdd:COG3599 109 EKARKIVREIEELKR 123
|
|
| FliH |
COG1317 |
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular ... |
1486-1595 |
9.47e-03 |
|
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440928 [Multi-domain] Cd Length: 172 Bit Score: 39.14 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982223 1486 EEAQQRAQAALDKANASrgqVEQANQELRELIQNVKDFLSQegadpdSIEMVATRVLDISIPASPEQIQRLASEIAERVR 1565
Cdd:COG1317 29 AEAEAEIAEALEQLQAL---LEQLQAPLEELDEELEEELVE------LALAIARKVIGRELALDPEAILALVREALAALR 99
|
90 100 110
....*....|....*....|....*....|
gi 31982223 1566 SLADVdTILAHTmGDVRRAEQLLQDAHRAR 1595
Cdd:COG1317 100 EAEEV-TIRVNP-DDLELVREALDELLGEG 127
|
|
| |
